https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Adis+Hasic 2026-09-15T03:55:54Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037764 2019-05-04T00:32:04Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome ''C''==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This &lt;scene name='Sandbox_Reserved_335/Axial/6'&gt;heme prosthetic&lt;/scene&gt; group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two unique structures of Cytochrome ''C'' exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;basic structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to four methionine <br /> groups on the occupied side of the heme group. When drawn out, the structure of <br /> Cytochrome ''C'' looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome ''C'' function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the Cytochrome ''C'' protein within the <br /> cell. Monoheme Cytochrome ''C'', which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome ''C'' is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;Cytochrome ''C'' protein in mitochondria&lt;/scene&gt;, <br /> one conformation of Cytochrome ''C'' is also a member of the electron transport chain in <br /> photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.) <br /> Cytochrome ''C'' is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome ''C'' plays a key role in the <br /> initiation of cell death. Without Cytochrome ''C'', the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome ''C'' takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome ''C'' to be released into the Cytosol. Once cytochrome ''C'' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome ''C'' which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome ''C'', intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in Cytochrome ''C'' causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome ''C'' also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome ''C'' accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the Cytochrome ''C'' release their electron that they <br /> are carrying and it is given to the Cytochrome ''C'' Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome ''C'' is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome ''C''. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome ''C'' reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome ''C'' then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome ''C'' to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome ''C'', but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of Cytochrome ''C''. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037763 2019-05-04T00:30:44Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome ''C''==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This &lt;scene name='Sandbox_Reserved_335/Axial/6'&gt;heme prosthetic&lt;/scene&gt; group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two unique structures of Cytochrome ''C'' exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;basic structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to four methionine <br /> groups on the occupied side of the heme group. When drawn out, the structure of <br /> Cytochrome ''C'' looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome ''C'' function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the Cytochrome ''C'' protein within the <br /> cell. Monoheme Cytochrome ''C'', which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome ''C'' is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the Cytochrome ''C'' protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of Cytochrome ''C'' is also a member of the electron transport chain in <br /> photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.) <br /> Cytochrome ''C'' is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome ''C'' plays a key role in the <br /> initiation of cell death. Without Cytochrome ''C'', the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome ''C'' takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome ''C'' to be released into the Cytosol. Once cytochrome ''C'' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome ''C'' which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome ''C'', intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in Cytochrome ''C'' causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome ''C'' also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome ''C'' accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the Cytochrome ''C'' release their electron that they <br /> are carrying and it is given to the Cytochrome ''C'' Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome ''C'' is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome ''C''. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome ''C'' reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome ''C'' then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome ''C'' to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome ''C'', but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of Cytochrome ''C''. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037762 2019-05-04T00:16:37Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome ''c''==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome &quot;C&quot; is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome 'C' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This &lt;scene name='Sandbox_Reserved_335/Axial/6'&gt;heme prosthetic&lt;/scene&gt; group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two unique structures of Cytochrome 'C' exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;basic structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to four methionine <br /> groups on the occupied side of the heme group. When drawn out, the structure of <br /> Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome 'C' function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the Cytochrome 'C' protein within the <br /> cell. Monoheme Cytochrome 'C', which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome 'C' is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the Cytochrome 'C' protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of Cytochrome 'C' is also a member of the electron transport chain in <br /> photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.) <br /> Cytochrome 'C' is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the <br /> initiation of cell death. Without Cytochrome 'C', the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome 'C' takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome 'C' to be released into the Cytosol. Once cytochrome 'C' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome 'C' which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome 'C', intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in Cytochrome 'C' causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome 'C' also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome 'C' accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the Cytochrome 'C' release their electron that they <br /> are carrying and it is given to the Cytochrome 'C' Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome 'C' is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome 'C'. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome 'C' reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome 'C' then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome 'C' to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome 'C', but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of Cytochrome 'C'. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037761 2019-05-04T00:15:34Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome &quot;C&quot;==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome &quot;C&quot; is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome 'C' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This &lt;scene name='Sandbox_Reserved_335/Axial/6'&gt;heme prosthetic&lt;/scene&gt; group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two unique structures of Cytochrome 'C' exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;basic structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to four methionine <br /> groups on the occupied side of the heme group. When drawn out, the structure of <br /> Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome 'C' function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the Cytochrome 'C' protein within the <br /> cell. Monoheme Cytochrome 'C', which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome 'C' is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the Cytochrome 'C' protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of Cytochrome 'C' is also a member of the electron transport chain in <br /> photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.) <br /> Cytochrome 'C' is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the <br /> initiation of cell death. Without Cytochrome 'C', the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome 'C' takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome 'C' to be released into the Cytosol. Once cytochrome 'C' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome 'C' which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome 'C', intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in Cytochrome 'C' causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome 'C' also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome 'C' accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the Cytochrome 'C' release their electron that they <br /> are carrying and it is given to the Cytochrome 'C' Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome 'C' is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome 'C'. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome 'C' reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome 'C' then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome 'C' to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome 'C', but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of Cytochrome 'C'. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037760 2019-05-04T00:05:54Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome 'C'==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome 'C' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome 'C' cause it to have different functions overall. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This &lt;scene name='Sandbox_Reserved_335/Axial/6'&gt;heme prosthetic&lt;/scene&gt; group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two unique structures of Cytochrome 'C' exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;basic structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to four methionine <br /> groups on the occupied side of the heme group. When drawn out, the structure of <br /> Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome 'C' function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the Cytochrome 'C' protein within the <br /> cell. Monoheme Cytochrome 'C', which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome 'C' is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the Cytochrome 'C' protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of Cytochrome 'C' is also a member of the electron transport chain in <br /> photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.) <br /> Cytochrome 'C' is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the <br /> initiation of cell death. Without Cytochrome 'C', the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome 'C' takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome 'C' to be released into the Cytosol. Once cytochrome 'C' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome 'C' which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome 'C', intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in Cytochrome 'C' causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome 'C' also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome 'C' accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the Cytochrome 'C' release their electron that they <br /> are carrying and it is given to the Cytochrome 'C' Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome 'C' is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome 'C'. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome 'C' reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome 'C' then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome 'C' to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome 'C', but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of Cytochrome 'C'. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037759 2019-05-03T21:29:06Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome 'C'==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome 'C' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome 'C' cause it to have different functions overall. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of Cytochrome 'C' exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome 'C' function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the Cytochrome 'C' protein within the <br /> cell. Monoheme Cytochrome 'C', which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome 'C' is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the Cytochrome 'C' protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of Cytochrome 'C' is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> Cytochrome 'C' is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the <br /> initiation of cell death. Without Cytochrome 'C', the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome 'C' takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome 'C' to be released into the Cytosol. Once cytochrome 'C' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome 'C' which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome 'C', intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in Cytochrome 'C' causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome 'C' also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome 'C' accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the Cytochrome 'C' release their electron that they <br /> are carrying and it is given to the Cytochrome 'C' Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome 'C' is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome 'C'. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome 'C' reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome 'C' then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome 'C' to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome 'C', but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of Cytochrome 'C'. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037757 2019-05-03T20:21:22Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally but both having the same general motif or &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037756 2019-05-03T20:20:41Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally but both having the same general &lt;scene name='Sandbox_Reserved_335/Motif/1'&gt;structure&lt;/scene&gt;. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_c&diff=3037755 2019-05-03T20:19:46Z

<p>Adis Hasic: </p> <hr /> <div>&lt;StructureSection load='' size='350' side='right' scene='Cytochrome_c/Cyt_c/1' caption='Cytochrome c with heme complex with sulfate (PDB code [[3cp5]])'&gt;<br /> The '''cytochrome ''c''''' (cyt ''c'') proteins are a superfamily belonging to the class of [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins], which are denoted as such by having an α-helical core. Each protein in this superfamily also contains one or more covalently-bound [http://en.wikipedia.org/wiki/Heme heme prosthetic groups].&lt;ref&gt;PMID:11697912&lt;/ref&gt;&lt;ref name=main /&gt; The cyt ''c'' superfamily contains many different families, some of which are better characterized than others. These families include monodomain and multi-domain C-type cytochromes, such as [http://proteopedia.org/wiki/index.php/1etp cyt c4], a diheme C-type cytochrome, and [http://proteopedia.org/wiki/index.php/2ozy NrfB], a pentaheme C-type cytochrome. In particular, the monoheme cyt ''c'' from ''Rhodothermus marinus'' has been previously studied and provides an excellent example of how some protein characteristics and structures can be extremely diverse, yet conserved, through evolution.&lt;br /&gt; For details on decaheme cyt see [[MtrF]].&lt;br /&gt; For details on Cyt c7 see [[Cytochrome c 7]].<br /> <br /> == Introduction ==<br /> <br /> [http://en.wikipedia.org/wiki/Cytochrome Cytochromes] are a class of heme-containing proteins found in bacteria and the mitochondria of eukaryotes.&lt;ref name=main /&gt; These proteins are generally membrane-bound and are known as respiratory pigments because they are involved in various electron transport systems in oxidative phosphorylation.&lt;ref name=&quot;heme&quot;&gt;PMID:14871137&lt;/ref&gt; Cytochromes can be categorized into several different types, three of which are based on the type of heme group the cytochrome contains: cytochromes ''a'', ''b'' and ''d'' contain heme ''a'', ''b'' and ''d'', respectively.&lt;ref name=amb /&gt; Cytochrome ''c'' is named such because it contains the heme ''c'', but is mainly distinguished from cytochromes ''a'', ''b'' and ''d'' due to the heme being coordinated with the protein scaffold by cysteinyl residues covalently bound to either one or both of the heme's vinyl side chains.&lt;ref name=heme /&gt; <br /> <br /> Cyt ''c'' has been split into four classes.&lt;ref name=amb&gt;PMID:1646017&lt;/ref&gt; Class I contains soluble, low spin&lt;ref name=main /&gt; single domain C-type cytochromes, of which there has been at least six subclasses found in prokaryotes including [http://en.wikipedia.org/wiki/Desulfovibrio ''Desulfovibrio desulfuricans''], [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum ''Rhodospirillum rubrum''], and ''Rhodothermus marinus''. Cyt ''c'' in this class have a single heme attached close to the N-terminus of the polypeptide, with a methionine residue being the sixth iron coordination site. Class II contains higher spin-state cytochromes ''c'', such as cyt ''c''', with the heme being attached closer to the C-terminus. Class III contains cytochromes with multiple heme groups; these proteins have lower redox potentials compared to the other three classes&lt;ref name=amb /&gt;. Finally, Class IV is comprised of more complex proteins with higher molecular weights containing heme ''c'' as well as other prosthetic groups.&lt;ref name=class&gt;Cookson DJ, Moore GR, Pitt RC, Williams RJP, Campbell ID, Ambler RP, Bruschi M, Le Gall J. Structural homology of cytochromes c. Eur J Biochem. 1978 Feb;83(1):261-75.&lt;/ref&gt;<br /> <br /> == ''Rhodothermus marinus'' cytochrome ''c'' ==<br /> <br /> == Structure ==<br /> <br /> &lt;scene name='Sandbox_Reserved_335/Heme/1'&gt;'Figure 1. The heme group of monoheme cytochrome ''c'' purified from ''Rhodothermus marinus''&lt;/scene&gt;<br /> <br /> All members in the C-type cytochrome superfamily contain a heme prosthetic group that is covalently attached to the protein via two thioether bonds to cysteine residues. Most cytochromes ''c'' occur in a where the histidine residue is one of the two axial ligands of the heme iron.&lt;ref name=main&gt;PMID:18855424&lt;/ref&gt;&lt;ref name=heme /&gt; In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or lysine residues.&lt;ref name=main /&gt;. In ''Rm''cyt''c'', XX represents a threonine (Thr46) and an alanine residue (Ala47) that help form the loop 2 structure.<br /> <br /> [[Image:heme.gif |frame|left| Figure 2. The tetrapyrrolic heme prosthetic group that can either be covalently attached to or closely associated with various proteins, such as cytochromes and other globin proteins. In ''Rm''cyt''c'', R2 is an ethyl group covalently attached to Cys 45, and R3 is a methyl group covalently attached to Cys48.]]<br /> {{Clear}}<br /> The typical monoheme cyt ''c'' fold is formed by helices &lt;scene name='Sandbox_Reserved_335/Helices/4'&gt;A, C, and E&lt;/scene&gt;. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, all connected by random coils.&lt;ref name=main /&gt; The heme group is axially coordinated by &lt;scene name='Sandbox_Reserved_335/Axial/6'&gt;His49 and Met100&lt;/scene&gt;, and the disulfide linkages exist at &lt;scene name='Sandbox_Reserved_335/Cys/1'&gt;Cys45 and Cys48&lt;/scene&gt;. The heme group in ''Rm''cyt''c'' is almost completely shielded from solvent due to it being in a mostly hydrophobic pocket. This pocket is formed in part by the seven helices surrounding the ring, but also by two structures that are uncommon in other cytochromes ''c''. First, a 21 amino acid extension of the N-terminal exists, forming &lt;scene name='Sandbox_Reserved_335/Uncommon1/2'&gt;α-helix A' and loop 1&lt;/scene&gt;, which wraps around the back of the polypeptide.&lt;ref name=main /&gt; An extension resembling such has only been seen in ''Thermus thermophilus''; however, the extension occurs at the C-terminus rather than the N-terminus.&lt;ref&gt;doi:10.1006/jmbi.1997.1181&lt;/ref&gt; A second rarity is that of &lt;scene name='Sandbox_Reserved_335/Uncommon2/2'&gt;helix B'&lt;/scene&gt;, inserted between helix D and loop 3, that shields the bottom part of the heme from any solvent.&lt;ref name=main /&gt; In cytochrome ''c''&lt;sub&gt;2&lt;/sub&gt; as well as mitochondrial cyt ''c'', a similar yet shorter helix was found, though this helix was present at a different place in the primary sequence. Also, instead of helix B', ''T. thermophilus'' contains a two-stranded [http://en.wikipedia.org/wiki/Beta_sheet β-sheet].&lt;ref name=main /&gt; One final note is the number of &lt;scene name='Sandbox_Reserved_335/Met/1'&gt;methionine&lt;/scene&gt; residues that ''Rm''cyt''c'' contains. In general, cyt ''c'' contains about two methionines whereas ''Rm''cyt''c'' contains seven, located on the left of the heme.&lt;ref name=main /&gt;<br /> <br /> As determined by X-ray crystallography, the ''Rm''cyt''c'' structure was found to contain a sulfate ion coordinated to Glu122 via hydrogen bonding to the protonated carboxylate oxygen. In the protein complex, this ion has been seen to mediate crystal contact between neighbouring protein molecules.&lt;ref name=main /&gt; <br /> <br /> The observation of these structural motifs in other C-type cytochromes can support the divergent evolution of cytochromes ''c''.&lt;ref name=main /&gt; These motifs are present in a number of different bacteria and are seen in similar regions of the secondary structure; however, they exist in the primary sequence in places distinct to the phylum. For example, monoheme cytochromes ''c'' in the rest of the Bacteroidetes phylum have an N-terminus extension that is highly conserved to that of ''Rm''cyt''c'', and the regions in the primary structure that correspond to these secondary motifs are not observed in other bacterial phyla.&lt;ref name=main /&gt; Also, due to these motifs being absent from other phyla, the Bacteroidetes monoheme cyt ''c'' has been said to form a new subfamily of cyt ''c''.<br /> <br /> == Function ==<br /> <br /> Monoheme cytochromes ''c'' are involved in electron transport chains in both prokaryotes and eukaryotic mitochondria.&lt;ref name=main /&gt; They mediate the transfer of electrons mainly from the ''bc''&lt;sub&gt;1&lt;/sub&gt; complexes or their analogs to heme-copper oxygen reductases (HCOs) in the [http://en.wikipedia.org/wiki/Electron_transport_chain electron transport chain] of [http://en.wikipedia.org/wiki/Oxidative_phosphorylation oxidative phosphorylation]. Heme ''c'' containing domains are often found fused to other protein domains such as these HCOs, including the ''caa''&lt;sub&gt;3&lt;/sub&gt; oxygen reductases&lt;ref name=main /&gt;&lt;ref&gt;PMID:14691678&lt;/ref&gt;; these enzymes are membrane-bound and catalyze the reduction of O&lt;sub&gt;2&lt;/sub&gt; to water.&lt;ref&gt;PMID:11334784&lt;/ref&gt; In addition to being involved in oxidative phosphorylation, monoheme cyt ''c'' has also been seen to participate in the electron transport chain of [http://en.wikipedia.org/wiki/Photosynthesis photosynthesis].&lt;ref name=main /&gt; Cytochrome ''c'' has also been determined to be a major signalling molecule in the apoptotic pathways.<br /> <br /> == Electron transport chain ==<br /> <br /> In the electron transport chain (ETC), cyt ''c'' shuttles electrons between the respiratory complexes III and IV; complex III is the cytochrome ''bc''&lt;sub&gt;1&lt;/sub&gt; complex and IV is cyt ''c'' oxidase. Initially, the heme iron in cyt ''c'' is in the reduced, Fe&lt;sup&gt;3+&lt;/sup&gt; state; this allows for the uptake of one electron, oxidizing the iron to the Fe&lt;sup&gt;2+&lt;/sup&gt; state.&lt;ref name='etc'&gt;Karp, Gerald (2008). Cell and Molecular Biology (5th edition). Hoboken, NJ: John Wiley &amp; Sons. ISBN 978-0470042175.&lt;/ref&gt; The ETC in eukaryotes is quite simple compared to that of prokaryotes (Figure 3). <br /> [[Image:Etc.gif |frame|left|thumb|300px| Figure 3. The electron transport chain of a) eukaryotes as compared to b) prokaryotes.]] <br /> <br /> In prokaryotic systems, electrons can enter the ETC at a number of places and multiple donors can be in play; however, the underlying transport system remains the same. Electrons are ultimately transferred from donor to various redox complexes including the ''bc''&lt;sub&gt;1&lt;/sub&gt; complex and cytochrome ''c'', and finally to a terminal electron acceptor such as molecular oxygen in eukaryotes.&lt;ref name=etc /&gt;<br /> <br /> The cytochrome oxidase reaction accounts for nearly 90% of all oxygen uptake in most cells.&lt;ref name=etc /&gt; Due to the large role of cytochromes within the ETC, it would be highly detrimental to the cell if any inhibitors were to be present in the organism. Cyanide and azide bind tightly to the cytochrome oxidase complex, halting electron transport and reducing the overall ATP production.&lt;ref name=etc /&gt;<br /> <br /> == Apoptosis ==<br /> <br /> In all organisms, cells undergo [http://en.wikipedia.org/wiki/Apoptosis apoptosis], or programmed cell death, by which there is an extrinsic and an intrinsic pathway. The extrinsic pathway involves an immune response by killer lymphocytes, and once the lymphocyte has been bound to the target cell, an apoptotic cascade occurs.&lt;ref name=etc /&gt; The intrinsic pathway includes cyt ''c'', present in the intermembrane space of mitochondria. In this pathway, the presence of an apoptotic stimulus causes cyt ''c'' to be released into the cytosol. Cytochrome ''c'' in the cytosol now can be recognized and bound to various apoptotic factors, activating them and forming the [http://en.wikipedia.org/wiki/Apoptosome apoptosome]. The apoptosome recruits [http://en.wikipedia.org/wiki/Caspase caspases], which are activated and result in a caspase cascade to proceed with apoptosis.&lt;ref name=etc /&gt;<br /> <br /> Cytochrome ''c'' is required for the intrinsic apoptotic process to function properly. Such as with the electron transport chain, a mutation affecting cyt ''c'' or other structures in apoptosis could cause either an increase or a decrease in the rate of apoptosis.<br /> <br /> ==Structural and kinetic studies of imidazole binding to two members of the cytochrome c6 family reveal an important role for a conserved heme pocket residue&lt;ref&gt;DOI 10.1007/s00775-011-0758-y&lt;/ref&gt;==<br /> <br /> &amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&lt;scene name='Journal:JBIC:7/Cv/4'&gt;Cytochrome c6&lt;/scene&gt; is a member of the class I family of c-type cytochromes with a distinctive &lt;scene name='Journal:JBIC:7/Cv/5'&gt;α-helical fold&lt;/scene&gt; and a &lt;scene name='Journal:JBIC:7/Cv/6'&gt;methionine and histidine residue serving as axial heme iron ligands&lt;/scene&gt;. They function in the photosynthetic electron transport chain of cyanobacteria where they shuttle an electron from the cytochrome b6f complex to photosystem I. Structures of numerous cytochrome ''c''&lt;sub&gt;6&lt;/sub&gt; proteins have been determined and all have the &lt;scene name='Journal:JBIC:7/Cv/7'&gt;methionine ligand coordinating to the iron&lt;/scene&gt;. In the present work we have solved the structure of the '''Q51V''' site-directed variant of ''Phormidium laminosum'' cytochrome ''c''&lt;sub&gt;6&lt;/sub&gt;. This project is part of a study that is aimed at gaining insight into protein factors which modulate the heme mid-point redox potential in the cytochrome ''c''&lt;sub&gt;6&lt;/sub&gt; family. The '''Q51V''' variant has been shown to tune over 100 mV of heme redox potential, which for a single heme pocket mutation is very significant and has consequences for function.<br /> <br /> &amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;The '''Q51V''' structure confirms that the &lt;scene name='Journal:JBIC:7/Cv/8'&gt;Val replacing the Gln&lt;/scene&gt; has the same side-chain orientation in the heme pocket as found in other cytochrome ''c''&lt;sub&gt;6&lt;/sub&gt; proteins, that naturally have a Val at this position. The significance of this structure is that the &lt;scene name='Journal:JBIC:7/Cv/14'&gt;axial heme iron methionine is dissociated&lt;/scene&gt; and an &lt;scene name='Journal:JBIC:7/Cv/15'&gt;exogenous ligand present in the crystallisation solution, imidazole, is now bound to the heme iron&lt;/scene&gt;. Two other structures of imidazole cyt c-adducts have been reported, but neither appear to undergo the &lt;scene name='Journal:JBIC:7/Cv/17'&gt;large structural changes seen in the Q51V structure&lt;/scene&gt;. Both protein and heme structural changes are observed, with the later centered on a &lt;scene name='Journal:JBIC:7/Cv/22'&gt;180 degree rotation around the CA atom of the two heme propionate groups&lt;/scene&gt; accompanied by the &lt;scene name='Journal:JBIC:7/Cv/20'&gt;upward movement of an alpha helix&lt;/scene&gt; and the &lt;scene name='Journal:JBIC:7/Cv/21'&gt;displacement of two loop regions&lt;/scene&gt;.<br /> <br /> &amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;&amp;nbsp;Protein (un)folding studies on cytochrome c have revealed that (un)folding involves structural units called 'foldons'. The regions in the Q51V imidazole-adduct where structural changes occur map well to the two foldons predicted to unfold first in cytochrome c. Thus &lt;scene name='Journal:JBIC:7/Cv/14'&gt;imidazole triggers the release of the methionine ligand in the Q51V variant&lt;/scene&gt;, leading to the formation of an early unfolding intermediate that is stabilised by &lt;scene name='Journal:JBIC:7/Cv/15'&gt;imidazole binding to the vacant heme iron coordination position&lt;/scene&gt;, enabling it to be captured in the crystalline form. <br /> <br /> ==Structural model of the [Fe]-hydrogenase/cytochrome C553 complex combining NMR and soft-docking&lt;ref&gt;PMID:10748163&lt;/ref&gt;==<br /> The &lt;scene name='1e08/1e08-cofactors/1'&gt;complex&lt;/scene&gt; shows the specific interaction of the hydrogenase (light blue) with the cytochrome (pink), revealing the path of electron transport from the &lt;scene name='1e08/1e08-activecluster/3'&gt;active site metal cluster&lt;/scene&gt;, through three iron-sulfur clusters, and ending in the cytochrome heme (colored red). Two &lt;scene name='1e08/1e08-cys/2'&gt;cysteine amino acids at the interface&lt;/scene&gt;, CYS 38 in the hydrogenase and CYS10 in the cytochrome, are thought to provide the electron transfer pathway between the two proteins (these scenes were created by Jaime Prilusky, David S. Goodsell, and Eran Hodis).<br /> <br /> == Conformational control of the binding of diatomic gases to cytochrome c’ &lt;ref&gt;PMID 25792378 &lt;/ref&gt;==<br /> <br /> The cytochromes c′ (CYTcp) are found in denitrifying, methanotrophic and photosynthetic bacteria. These proteins are able to form stable adducts with CO and NO but not with O2. The binding of NO to CYTcp currently provides the best structural model for the NO activation mechanism of soluble guanylate cyclase. Ligand binding in CYTcps has been shown to be highly dependent on residues in both the proximal and distal heme pockets. Group 1 CYTcps typically have a phenylalanine residue positioned close to the distal face of heme, while for group 2, this residue is typically leucine. We have structurally, spectroscopically and kinetically characterised the CYTcp from ''Shewanella frigidimarina'' &lt;scene name='69/696899/Cv/2'&gt;(SFCP)&lt;/scene&gt;, a protein that has a distal phenylalanine residue and a lysine in the proximal pocket in place of the more common arginine (&lt;font color='red'&gt;&lt;b&gt;monomer A is colored in red&lt;/b&gt;&lt;/font&gt;, &lt;span style=&quot;color:lime;background-color:black;font-weight:bold;&quot;&gt;monomer B in green&lt;/span&gt;, and &lt;span style=&quot;color:yellow;background-color:black;font-weight:bold;&quot;&gt;heme group in yellow&lt;/span&gt;). &lt;scene name='69/696899/Cv/3'&gt;Each monomer of the SFCP dimer folds as a 4-alpha-helical bundle&lt;/scene&gt; in a similar manner to CYTcps previously characterised. <br /> * &lt;scene name='69/696899/Cv/4'&gt;Heme group and its environment in as-isolated SFCP&lt;/scene&gt;.<br /> * &lt;scene name='69/696899/Cv/5'&gt;Proximal NO complex of SFCP (monomer A)&lt;/scene&gt;.<br /> * &lt;scene name='69/696899/Cv/8'&gt;Click here to see the difference between these structures&lt;/scene&gt;.<br /> SFCP exhibits biphasic binding kinetics for both NO and CO as a result of the high level of steric hindrance from the aromatic side chain of residue Phe 16. The binding of distal ligands is thus controlled by the conformation of the phenylalanine ring. <br /> * &lt;scene name='69/696899/Cv/12'&gt;A superposition of the heme environments&lt;/scene&gt; of &lt;span style=&quot;color:lime;background-color:black;font-weight:bold;&quot;&gt;SFCP (in green&lt;/span&gt;;[[4ulv]]), &lt;font color='magenta'&gt;&lt;b&gt;RCCP (''R. capsulatus''; in magenta&lt;/b&gt;&lt;/font&gt;; [[1cpq]]), &lt;font color='red'&gt;&lt;b&gt;RSCP (''R. sphaeroides''; in red&lt;/b&gt;&lt;/font&gt;; [[1gqa]]) and &lt;span style=&quot;color:cyan;background-color:black;font-weight:bold;&quot;&gt;RGCP (''R. gelatinosus''; in cya)&lt;/span&gt;; [[2j8w]]).<br /> * &lt;scene name='69/696899/Cv/14'&gt;Click here to see morph of this scene&lt;/scene&gt;.<br /> Only a proximal 5-coordinate NO adduct, confirmed by structural data, is observed with no detectable hexacoordinate distal NO adduct.<br /> &lt;/StructureSection&gt;<br /> <br /> ==3D structures of cytochrome C==<br /> <br /> Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}<br /> {{#tree:id=OrganizedByTopic|openlevels=0|<br /> <br /> *Cytochrome C<br /> <br /> **[[3nwv]], [[3zoo]] – hCyt (mutant) – human&lt;BR /&gt;<br /> **[[3zcf]] – hCyt&lt;br /&gt;<br /> **[[1j3s]] – hCyt - NMR&lt;BR /&gt;<br /> **[[3nbs]], [[3nbt]], [[1crc]], [[1hrc]], [[3o1y]], [[3o20]], [[3wc8]], [[3wui]], [[4rsz]] – hoCyt – horse&lt;BR /&gt;<br /> **[[1lc1]], [[1lc2]], [[1m60]], [[1giw]], [[2giw]], [[1akk]], [[2frc]], [[1ocd]] – hoCyt – NMR&lt;BR /&gt;<br /> **[[1fi9]], [[1fi7]] - hoCyt + imidazole – NMR&lt;BR /&gt;<br /> **[[1u75]] - hoCyt + Cyt peroxidase&lt;BR /&gt;<br /> **[[1wej]] – hoCyt + Fab fragment&lt;BR /&gt;<br /> **[[3a9f]] – CtCyt C-terminal – ''Chlorobaculum tepidum''&lt;BR /&gt;<br /> **[[3cp5]] – Cyt residues 29-152 – ''Rhodothermus marinus''&lt;BR /&gt;<br /> **[[2jti]], [[3tyi]] – yCyt (mutant) + Cyt peroxidase – yeast&lt;BR /&gt;<br /> **[[2pcb]] - yCyt + Cyt peroxidase&lt;BR /&gt;<br /> **[[2gb8]] - yCyt + Cyt peroxidase - NMR&lt;BR /&gt;<br /> **[[2jqr]] - yCyt (mutant) + adrenodoxin&lt;BR /&gt;<br /> **[[2orl]] - yCyt (mutant) – NMR&lt;BR /&gt;<br /> **[[1crg]], [[1crh]], [[1cri]], [[1crj]], [[ 2ycc]] - yCyt&lt;BR /&gt;<br /> **[[1ytc]], [[1cie]], [[1cif]], [[1cig]], [[1cih]], [[1csu]], [[1csv]], [[1csw]], [[1csx]], [[1chh]], [[1chi]], [[1chj]], [[1cty]], [[1ctz]] - yCyt (mutant)&lt;br /&gt;<br /> **[[1rap]], [[1raq]], [[1ycc]]- yCyt iso-1&lt;BR /&gt;<br /> **[[1yic]] – yCyt iso-1 – NMR&lt;BR /&gt;<br /> **[[1irv]], [[1irw]], [[1lms]], [[4mu8]], [[4n0k]] – yCyt iso-1 (mutant) &lt;BR /&gt;<br /> **[[2hv4]], [[2lir]], [[2lit]], [[2mhm]] - yCyt iso-1 (mutant) - NMR&lt;br /&gt;<br /> **[[1fhb]] - yCyt iso-1 (mutant) + CN - NMR&lt;BR /&gt;<br /> **[[1nmi]] – yCyt iso-1 + imidazole&lt;BR /&gt;<br /> **[[2b0z]], [[2b10]], [[2b11]], [[2b12]], [[1u74]], [[1s6v]], [[2bcn]] – yCyt iso-1 (mutant) + Cyt peroxidase&lt;BR /&gt;<br /> **[[2pcc]] – yCyt iso-1 + Cyt peroxidase&lt;BR /&gt;<br /> **[[1yea]], [[1yeb]] – yCyt iso-2&lt;BR /&gt;<br /> **[[2e84]] – DvCyt – ''Desulfovibrio vulgaris''&lt;BR /&gt;<br /> **[[2j7a]] – DvCyt catalytic + electron donor subunits&lt;BR /&gt;<br /> **[[2oz1]] – RsuCyt – ''Rhodovulum sulfidophilum''&lt;BR /&gt;<br /> **[[1h31]], [[1h32]], [[1h33]] – RsuCyt diheme&lt;br /&gt;<br /> **[[2aiu]] – Cyt – mouse&lt;BR /&gt;<br /> **[[2fw5]], [[2fwt]] – RsCyt diheme residues 1-139 - ''Rhodobacter sphaeroides''&lt;BR /&gt;<br /> **[[1dw0]], [[1dw3]] - RsCyt diheme residues 1-112&lt;BR /&gt;<br /> **[[1dw1]], [[1dw2]] - RsCyt diheme residues 1-112 + small molecule&lt;BR /&gt;<br /> **[[1ogy]] - RsCyt diheme residues 25-154 + nitrate reductase catalytic subunit&lt;BR /&gt;<br /> **[[2a3m]], [[2a3p]] – DdCyt tetraheme membrane-bound subunit - ''Desulfovibrio desulfuricans''&lt;BR /&gt;<br /> **[[1h21]] - DdCyt di-heme&lt;BR /&gt;<br /> **[[1ofw]], [[1ofy]], [[1duw]], [[19hc]] - DdCyt nine-heme&lt;BR /&gt;<br /> **[[1oah]] - DdCyt&lt;BR /&gt;<br /> **[[2b4z]] – bCyt – bovine&lt;BR /&gt;<br /> **[[1lfm]], [[1i55]], [[3cyt]], [[1i54]], [[1i5t]] - Cyt – tuna&lt;BR /&gt;<br /> **[[1fs7]], [[1fs8]], [[1fs9]] – WsCyt + small molecule – ''Wolinella succinogenes''&lt;BR /&gt;<br /> **[[1dxr]] – RvCyt in photosynthetic reaction center – ''Rhodopseudomonas viridis''&lt;BR /&gt;<br /> **[[1qdb]] – Cyt – ''Sulfurospirillum deleyianum''&lt;BR /&gt;<br /> **[[5cyt]] – Cyt - albacore&lt;br /&gt;<br /> **[[2ccy]] – Cyt – ''Phaeospirillum molischianum''&lt;br /&gt;<br /> **[[4dy9]] – Cyt – ''Leishmania major''&lt;br /&gt;<br /> **[[3u99]] – Cyt diheme – ''Shewanella baltica''&lt;br /&gt;<br /> **[[3j2t]] – Cyt + apoptotic protease-activating factor 1 – bovine – Cryo EM&lt;br /&gt;<br /> <br /> *Cytochrome C’<br /> <br /> **[[2xl6]], [[2xld]], [[2xle]], [[2xlo]], [[2xlv]], [[2xlw]] – AxCyt (mutant) + NO – ''Achromobacter xylosoxidans''&lt;BR /&gt;<br /> **[[1cgn]], [[1cgo]], [[2ykz]], [[3zqv]], [[2yli]], [[4cda]], [[4cdv]], [[4cdy]], [[4cip]], [[4cjo]], [[4wgy]], [[4wgz]] - AxCyt&lt;BR /&gt;<br /> **[[2xm0]], [[2xm4]], [[2xl8]], [[2xlh]], [[2yl0]], [[2yl7]], [[3ztm]] - AxCyt (mutant) &lt;BR /&gt; <br /> **[[2yl1]], [[2yl3]], [[2ylg]], [[3zqy]], [[3ztz]] - AxCyt (mutant) + CO&lt;br /&gt;<br /> **[[2yld]], [[3zwi]] - AxCyt + CO&lt;br /&gt;<br /> **[[2xlm]], [[4cjg]] - AxCyt + NO&lt;BR /&gt;<br /> **[[2j9b]], [[2j8w]] – Cyt – ''Rubrivivax gelatinosus''&lt;BR /&gt;<br /> **[[1gqa]] – RsCyt&lt;BR /&gt;<br /> **[[1mqv]], [[1a7v]] – RpCyt – ''Rhodopseudomonas palustris''&lt;BR /&gt;<br /> **[[1eky]] – RcCyt]] - ''Rhodobacter capsulatus'' – NMR&lt;BR /&gt;<br /> **[[1cpr]], [[1cpq]], [[1rcp]] – RcCyt&lt;BR /&gt;<br /> **[[1nbb]] – RcCyt + cyanide&lt;BR /&gt;<br /> **[[1e83]], [[1e84]], [[1e85]], [[1e86]] – Cyt - ''Alcaligenes xylosoxidans''&lt;BR /&gt;<br /> **[[1jaf]] – Cyt – ''Rhodocyclus gelatinosus''&lt;BR /&gt;<br /> **[[1bbh]] – Cyt – ''Allochromatium vinosum''&lt;br /&gt;<br /> **[[3vcr]] - CtCyt&lt;br /&gt;<br /> **[[3vrc]] – Cyt – ''Thermochromatium tepidum''&lt;br /&gt;<br /> **[[4cx9]] - Cyt – ''Shewanella frigidimarina''&lt;br /&gt;<br /> **[[4ulv]] - Cyt + NO – ''Shewanella frigidimarina''&lt;br /&gt;<br /> <br /> *Cytochrome C’’<br /> <br /> **[[1oae]], [[1gu2]] – MmCyt – ''Methylophilus methylotrophus''&lt;BR /&gt;<br /> **[[1e8e]] – MmCyt - NMR&lt;BR /&gt;<br /> <br /> *Cytochrome C1<br /> <br /> **[[3cx5]], [[3cxh]] – yCyt in complex III&lt;BR /&gt;<br /> **[[2ibz]] - yCyt in complex III + inhibitor&lt;BR /&gt;<br /> **[[1kyo]] - yCyt in Bc1 complex&lt;BR /&gt;<br /> **[[1kb9]] – yCyt in Bc1 complex residues 17-368&lt;BR /&gt;<br /> **[[1ezv]] - yCyt in Bc1 complex + antibody FV fragment&lt;BR /&gt;<br /> **[[3h1h]], [[1bcc]] - cCyt in Bc1 complex – chicken&lt;BR /&gt;<br /> **[[3h1i]], [[2bcc]], [[3bcc]] - cCyt in Bc1 complex + inhibitor&lt;BR /&gt;<br /> **[[2qjk]], [[2qjp]], [[2qjy]] – RsCyt in Bc1 complex + inhibitor&lt;BR /&gt; <br /> **[[2fyn]] - RsCyt in Bc1 complex (mutant) &lt;BR /&gt;<br /> **[[1l0n]], [[1be3]], [[1bgy]], [[1qcr]] – bCyt in Bc1 complex&lt;BR /&gt;<br /> **[[2fyu]] - bCyt in Bc1 complex (mutant) + inhibitor&lt;BR /&gt; <br /> **[[1sqp]], [[1sqq]], [[1sqv]], [[1sqx]], [[2a06]], [[1sqb]], [[1pp9]], [[1ppj]], [[1ntk]], [[1ntm]], [[1p84]], [[1l0l]] - bCyt in Bc1 complex + inhibitor&lt;BR /&gt;<br /> **[[1ntz]], [[1nu1]] - bCyt in Bc1 complex + substrate&lt;BR /&gt;<br /> **[[1zrt]] - RcCyt in Bc1 complex + inhibitor&lt;br /&gt;<br /> **[[2yiu]] - PdCyt in Bc1 complex – ''Paracoccus denitrificans'' <br /> <br /> *Cytochrome C2<br /> <br /> **[[1c2r]] - RcCyt&lt;BR /&gt;<br /> **[[1vyd]] – RcCyt (mutant) &lt;BR /&gt;<br /> **[[1c2n]] – RcCyt - NMR&lt;BR /&gt;<br /> **[[1l9b]], [[1l9j]] – RsCyt in photosynthetic reaction center&lt;BR /&gt;<br /> **[[2cxb]], [[1cxc]], [[1cxa]] - RsCyt&lt;BR /&gt;<br /> **[[1jdl]] – Cyt – ''Rhodospirillum centenum''&lt;BR /&gt;<br /> **[[2c2c]], [[3c2c]] – Cyt – ''Rhodospirillum rubrum''&lt;BR /&gt;<br /> **[[1i8o]], [[1hh7]], [[1fj0]], [[1i8p]] – RpCyt&lt;BR /&gt;<br /> **[[1hro]] – Cyt – ''Rhodopila globiformis''&lt;BR /&gt;<br /> **[[1cot]] – PdCyt - ''Paracoccus denitrificans''&lt;BR /&gt;<br /> **[[1cry]] - RvCyt&lt;br /&gt;<br /> **[[1co6]], [[1io3]] – BvCyt - ''Blastochloris viridis''<br /> <br /> *Cytochrome C3<br /> <br /> **[[2ksu]], [[1up9]], [[1upd]], [[1gmb]], [[1gm4]], [[1i77]], [[3cyr]] – DdCyt&lt;BR /&gt; <br /> **[[2kmy]] – DdCyt – NMR&lt;BR /&gt;<br /> **[[2k3v]] – Cyt – ''Shewanella frigidimarina''&lt;BR /&gt;<br /> **[[1m1p]], [[1m1r]], [[1m1q]] - SoCyt tetraheme – ''Shewanella oneidensis''&lt;BR /&gt;<br /> **[[3pmq]] - SoCyt decaheme&lt;br /&gt;<br /> **[[1it1]] – DvCyt&lt;br /&gt;<br /> **[[2bpn]] – DvCyt fragment - NMR&lt;br /&gt;<br /> **[[1j0o]], [[2cth]], [[2cdv]] - DvCyt tetraheme&lt;BR /&gt;<br /> **[[2z47]], [[2yyw]], [[2yyx]], [[2yxc]], [[2ffn]], [[2ewi]], [[2ewk]], [[2ewu]], [[1wr5]], [[1j0p]], [[1mdv]], [[2cym]] – DvCyt tetraheme (mutant) &lt;BR /&gt;<br /> **[[1gx7]] – DvCyt + hydrogenase&lt;BR /&gt;<br /> **[[1gyo]], [[1wad]], [[1qn0]], [[1qn1]] - DgCyt di-tetraheme – ''Desulfovibrio gigas''&lt;BR /&gt;<br /> **[[1z1n]] - DgCyt sixteen heme&lt;br /&gt;<br /> **[[2bq4]], [[3cao]], [[3car]] – Cyt – ''Desulfovibrio africanus''&lt;BR /&gt;<br /> **[[1w7o]] - Cyt – ''Desulfomicrobium baculatus''&lt;BR /&gt;<br /> **[[1aqe]] – DnCyt (mutant) – ''Desulfomicrobium norvegicum''&lt;br /&gt;<br /> **[[1czj]], [[2cy3]] - DnCyt&lt;br /&gt;<br /> **[[1a2i]] - DvCyt&lt;br /&gt;<br /> **[[2ldo]] – GsCyt residues 21-91 – ''Geobacter sulfurreducens'' - NMR&lt;br /&gt;<br /> **[[2izz]] - GsCyt residues 21-91 (mutant) – NMR&lt;br /&gt;<br /> **[[3ov0]] – GsCyt residues 26-343 dodedcaheme&lt;br /&gt;<br /> **[[3ouq]] - GsCyt residues 26-186 hexaheme&lt;br /&gt;<br /> **[[3oue]] - GsCyt residues 186-343 hexaheme<br /> <br /> *Cytochrome C4<br /> <br /> **[[1m6z]], [[1m70]], [[1etp]] – PsCyt – ''Pseudomonas stutzeri''&lt;BR /&gt;<br /> **[[1h1o]] – Cyt - ''Acidithiobacillus ferrooxidans''<br /> <br /> *Cytochrome C5<br /> <br /> **[[1cc5]] – Cyt – ''Azotobacter vinelandii''<br /> <br /> *Cytochrome C6<br /> <br /> **[[3ph2]] – PlCyt (mutant) – ''Phormidium laminosum''&lt;BR /&gt;<br /> **[[3dr0]], [[4eic]], [[4eie]] – SyCyt – ''Synechococcus''&lt;BR /&gt;<br /> **[[4eid]], [[4eif]] – SyCyt (mutant)&lt;br /&gt;<br /> **[[3dmi]] – Cyt – ''Phaeodactylum tricornutum''&lt;BR /&gt;<br /> **[[2zbo]] – Cyt – ''Hizikia fusiformis''&lt;BR /&gt;<br /> **[[2v07]], [[2dge]] – AtCyt residues 71-175 – ''Arabidopsis thaliana''&lt;BR /&gt;<br /> **[[2ce0]], [[2ce1]] - AtCyt residues 71-175 (mutant) &lt;BR /&gt;<br /> **[[2v08]] – PlCyt &lt;BR /&gt;<br /> **[[1ls9]] – Cyt – ''Cladophora glomerata''&lt;BR /&gt;<br /> **[[1kib]], [[1f1f ]] – AmCyt – ''Arthrospira maxima''&lt;BR /&gt;<br /> **[[1gdv]] – Cyt – ''Porphyra yezoensis''&lt;BR /&gt;<br /> **[[1a2s]], [[1ced]] – MbCyt – ''Monoraphidium braunii'' – NMR&lt;BR /&gt;<br /> **[[1ctj]] - MbCyt&lt;BR /&gt;<br /> **[[1c6s]] – Cyt – ''Cyanobacterium synechococcus'' - NMR&lt;BR /&gt;<br /> **[[1c6o]], [[1c6r]] – Cyt – ''Scenedesmus obliquus''&lt;br /&gt;<br /> **[[1ccr]] – Cyt - rice&lt;br /&gt;<br /> **[[4gyd]] – noCyt – nostoc&lt;br /&gt;<br /> **[[4h0j]], [[4h0k]] – noCyt (mutant) &lt;br /&gt;<br /> <br /> *Cytochrome C7<br /> <br /> **[[3h33]], [[3h34]], [[3h4n]], [[3bxu]] – GsCyt &lt;BR /&gt;<br /> **[[1lm2]], [[1l3o]], [[1kwj]], [[1f22]], [[1ehj]] – DaCyt – ''Deulfurmonas acetoxidans'' – NMR&lt;BR /&gt;<br /> **[[1hh5]] - DaCyt&lt;br /&gt;<br /> **[[3sel]], [[3sj0]], [[3sj1]], [[3sj4]] – Cyt (mutant) – ''Geobascter desulfurreducens''&lt;br /&gt;<br /> <br /> *Cytochrome C549<br /> <br /> **[[1f1c]] – AmCyt&lt;BR /&gt;<br /> **[[1e29]] - SyCyt<br /> <br /> *Cytochrome C550<br /> <br /> **[[3wu2]], [[4v82]], [[3kzi]], [[3a0b]], [[3a0h]], [[4v62]], [[1izl]], [[5ws6]], [[5ws5]], [[5v2c]], [[5gti]], [[5gth]], [[5b66]], [[5b5e]], [[4ub8]], [[4ub6]], [[4il6]] – Cyt in photosystem II – ''Thermosynechococcus vulcanus''&lt;BR /&gt;<br /> **[[2axt]], [[1w5c]], [[1s5l]], [[5h2f]], [[5tis]], [[5mx2]], [[5kai]], [[5kaf]], [[5e7c]], [[5e79]], [[4tnk]], [[4tnj]], [[4tni]], [[4tnh]], [[4rvy]], [[4pj0]], [[4pbu]], [[4ixr]], [[4ixq]], [[4fby]] - TeCyt in photosystem II – ''Thermosynechococcus elongatus''&lt;BR /&gt;<br /> **[[2bgv]] – PvCyt – ''Paracoccus versutus''&lt;BR /&gt;<br /> **[[2bh4]], [[2bh5]] – PvCyt (mutant) &lt;BR /&gt;<br /> **[[1mz4]] – TeCyt&lt;BR /&gt;<br /> **[[155c]] - PdCyt<br /> <br /> *Cytochrome C551<br /> <br /> **[[2zon]] – AxCyt + nitrite reductase&lt;BR /&gt;<br /> **[[2gc7]], [[2gc4]], [[2mta]] – PdCyt + methylamine dehydrogenase + amicyanin&lt;BR /&gt;<br /> **[[1cch]], [[1cor]] – PsCyt - NMR&lt;BR /&gt; <br /> **[[1gks]] – Cyt – ''Ectothiorhodospira halophila'' - NMR&lt;BR /&gt;<br /> **[[1new]] – DaCyt triheme]- NMR&lt;BR /&gt;<br /> **[[2exv]] – PaCyt (mutant) – ''Pseudomonas aeruginosa''&lt;BR /&gt;<br /> **[[351c]], [[451c]] - PaCyt&lt;BR /&gt;<br /> **[[2pac]] – PaCyt - NMR&lt;BR /&gt;<br /> **[[1dvv]] - PaCyt (mutant) – NMR&lt;BR /&gt;<br /> **[[1fi3]], [[2i8f]] - PsCyt (mutant) – NMR&lt;br /&gt;<br /> **[[5xec]], [[5xed]] – Cyt551/Cyt552 – ''Hydrogenobacter thermophilus''&lt;br /&gt;<br /> <br /> *Cytochrome C552 [[Nitrite reductase]]<br /> <br /> *Cytochrome C553<br /> <br /> **[[1b7v]], [[1c75]] – BpCyt - ''Bacillus pasteuri''&lt;BR /&gt;<br /> **[[1k3h]], [[1k3g]] – BpCyt – NMR&lt;BR /&gt;<br /> **[[1e08]] – DdCyt + hydrogenase - NMR&lt;BR /&gt;<br /> **[[1n9c]] – Cyt – ''Sporosarcina pasteurii''&lt;BR /&gt;<br /> **[[1c53]] - DvCyt&lt;BR /&gt;<br /> **[[1dvh]] - DvCyt - NMR&lt;br /&gt;<br /> **[[2dvh]] - DvCyt (mutant) - NMR&lt;BR /&gt;<br /> **[[1dwl]] – DvCyt + ferredoxin I – NMR&lt;BR /&gt;<br /> **[[1cyi]], [[1cyj]] – Cyt – ''Chlamydomonas reinhardtii''<br /> <br /> *Cytochrome C554<br /> <br /> **[[2zzs]] – Cyt – ''Vibrio parahaemolyticus''&lt;BR /&gt;<br /> **[[1ft5]], [[1ft6]], [[1bvb]] – Cyt – ''Nitrosomonas europaea''<br /> <br /> *Cytochrome C555<br /> <br /> **[[2zxy]] – Cyt – ''Aquifex aeolicus''&lt;BR /&gt;<br /> **[[2yk3]] – Cyt – ''Crithidia fasciculate''&lt;br /&gt;<br /> **[[4j20]] – CtCyt (mutant)&lt;br /&gt;<br /> <br /> * Cytochrome C557<br /> <br /> **[[1foc]] – TtCyt – ''Thermus thermophilus''&lt;br /&gt;<br /> <br /> *Cytochrome C556<br /> <br /> **[[1s05]] – RpCyt - NMR&lt;BR /&gt;<br /> <br /> *Cytochrome C558<br /> <br /> **[[2x5u]], [[2x5v]] – BvCyt in photosynthetic reaction center – ''Blastochloris viridis'' – Laue&lt;BR /&gt;<br /> **[[2wjm]], [[2wjn]], [[3g7f]], [[3d38]], [[2jbl]], [[2i5n]], [[1vrn]], [[1r2c]] - BvCyt in photosynthetic reaction center <br /> <br /> *Cytochrome C562<br /> <br /> **[[3qvz]] – EcCyt + Cu + Zn <br /> <br /> *Cytochrome C NAPB<br /> <br /> **[[3ml1]], [[3o5a]] – Cyt + nitrate reductase catalytic subunit – ''Ralstonia eutropha''&lt;br /&gt;<br /> **[[1jni]] – Cyt small subunit – ''Haemophilus influenzae''<br /> <br /> *Cytochrome CL<br /> <br /> **[[2d0w]] – Cyt – ''Hyphomicrobium denitrificans''&lt;BR /&gt;<br /> **[[2c8s]] – MeCyt – ''Methylobacterium extorquens''&lt;br /&gt;<br /> **[[1mg2]], [[1mg3]] – PdCyt + methylamine hydrogenase + amicyanin&lt;br /&gt;<br /> <br /> *Cytochrome CC3<br /> <br /> **[[2cvc]], [[1gws]], [[1h29]] – DvCyt<br /> <br /> *Cytochrome CD1<br /> <br /> **[[1gq1]], [[1h9x]], [[1h9y]], [[1hcm]], [[1qks]] – Cyt – ''Paracoccus pantotrophus''&lt;BR /&gt;<br /> **[[1gjq ]]– PaCyt&lt;BR /&gt; <br /> **[[1dy7]] – PaCyt + CO&lt;BR /&gt;<br /> **[[1e2r]] – PdCyt + CN <br /> <br /> *Cytochrome CH<br /> <br /> **[[1qn2]] – MeCyt <br /> <br /> *Cytochrome CB562<br /> <br /> **[[3qvy]], [[3qw0]], [[3qw1]] – EcCyt + Zn&lt;br /&gt;<br /> **[[3c62]], [[3c63]], [[3iq5]], [[3iq6]], [[3l1m]], [[3m15]], [[3nmi]], [[3nmk]] - EcCyt (mutant) + Zn&lt;br /&gt;<br /> **[[3de8]], [[3m79]] - EcCyt (mutant) + Zn + Cu&lt;br /&gt;<br /> **[[3de9]], [[3nmj]] - EcCyt (mutant) + Zn + Ni<br /> }}<br /> == References ==<br /> <br /> &lt;references/&gt;<br /> <br /> [[Category:Topic Page]]</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037754 2019-05-03T20:15:11Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''&gt;<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037753 2019-05-03T20:14:42Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='3CP5' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037752 2019-05-03T20:14:07Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037751 2019-05-03T20:13:37Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme prosthetic groups] protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037629 2019-05-03T02:18:59Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes the electron transport chain. Cytochrome C is an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4 <br /> electrons and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037623 2019-05-03T01:59:39Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 4 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037622 2019-05-03T01:58:39Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> A.j., et al. “Three-Dimensional Structure of Cytochrome c' from Two Alcaligenes Species and the Implications for Four-Helix Bundle Structures.” Acta Crystallogr.,Sect.D, www.rcsb.org/structure/1CGN.<br /> “Cytochrome C.” Cytochrome C - an Overview | ScienceDirect Topics, www.sciencedirect.com/topics/neuroscience/cytochrome-c.<br /> “Cytochrome c.” Cytochrome c - Proteopedia, Life in 3D, proteopedia.org/wiki/index.php/Cytochrome_c.<br /> Elmore, Susan. “Apoptosis: a Review of Programmed Cell Death.” Toxicologic Pathology, U.S. National Library of Medicine, 2007, www.ncbi.nlm.nih.gov/pmc/articles/PMC2117903/.<br /> Hüttemann, Maik, et al. “The Multiple Functions of Cytochrome c and Their Regulation in Life and Death Decisions of the Mammalian Cell: From Respiration to Apoptosis.” Mitochondrion, U.S. National Library of Medicine, May 2011, www.ncbi.nlm.nih.gov/pmc/articles/PMC3075374/.<br /> Ow, Yong-Ling P, et al. “Cytochrome c: Functions beyond Respiration.” Nature Reviews. Molecular Cell Biology, U.S. National Library of Medicine, July 2008, www.ncbi.nlm.nih.gov/pubmed/18568041.<br /> “PDB101: Molecule of the Month: Cytochrome c.” RCSB, pdb101.rcsb.org/motm/36.<br /> The Journal of Biochemistry, Volume 45, Issue 5, 1 May 1958, Pages 341–348,<br /> New Journal of Science, Volume 2014, Article ID 484538, 28 pages<br /> <br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037589 2019-05-02T21:31:50Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037588 2019-05-02T21:30:32Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1j3s' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> &lt;scene name='81/814739/Cytochrome_c/1'&gt;Cytochrome C&lt;/scene&gt; is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037492 2019-05-01T21:37:47Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> &lt;scene name='81/814739/Cytochrome_c/1'&gt;Cytochrome C&lt;/scene&gt; is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3037491 2019-05-01T21:33:23Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in &lt;scene name='81/814739/Bc1_complex_cytc/1'&gt;mitochondria&lt;/scene&gt;, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3033624 2019-04-24T15:33:46Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in mitochondria, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Purpose in ETC and Photosynthesis ==<br /> Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of <br /> the many electron carriers in the electron transport chain but quite a vital one. The heme group <br /> portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the <br /> electrons to complex IV. Once at complex IV, the cytochrome C release their electron that they <br /> are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme collects 4 <br /> electrons from 4 different Cytochrome C transport proteins and transfers them to one dioxygen <br /> molecule in order to make two molecules of water. It is also found within the thylakoid <br /> membrane in the chloroplast of plants, cyanobacteria, and green algae. In photosynthesis, <br /> Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I. <br /> Concurrently, it pumps protons across the thylakoid membrane adding in its own contribution <br /> into creating an electrochemical gradient. Later in the cycle, the electrochemical gradient will <br /> then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)<br /> <br /> == Medical/Research Purposes ==<br /> A proposal by many research scientists has been to regulate mitochondrial energy <br /> production and ROS production through the phosphorylation of cytochrome C. It has been <br /> observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is <br /> partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome <br /> c) They are proposing that “this effect plays an essential role in the prevention of ROS under <br /> healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then <br /> becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets <br /> up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial <br /> membrane potential differences and it needs to be taken into account to be able to determine the <br /> risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of <br /> Cytochrome C, but acknowledges the fact that other factors may also be affected through their <br /> actions. Others have began to focus their research on major diseases such as Huntington’s <br /> disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the <br /> closest that anyone has come to a universal cure for cancers has been with the use of the <br /> apoptotic function of cytochrome C. They went on to explain that tricking the body into <br /> believing these cancerous cells are ready to die, they could negate the effects of the ineffective <br /> p53 gene.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3033618 2019-04-24T15:31:01Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> Cytochrome C function is dependent on the conformation of the structure it is portraying <br /> at the time which is primarily determined by the location of the cytochrome c protein within the <br /> cell. Monoheme cytochrome C, which is primarily found in the mitochondria of the cell, <br /> functions in eukaryotes and prokaryotes during the electron transport chain. They are an electron <br /> transfer protein during the bc1 complex of the electron transport chain. (See below for more <br /> detailed information) Involving identical structure to the cytochrome C protein in mitochondria, <br /> one conformation of cytochrome C is also a member of the electron transport chain in <br /> photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.) <br /> You can also find it in a Heme C form which is a membrane bound protein that converts O2 into <br /> two water molecules using the electrons. Cytochrome C is also a main signaling factor for <br /> apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the <br /> initiation of cell death. Without Cytochrome C, the cell could not release the protein into the <br /> cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed <br /> information on this function)<br /> <br /> == Role in Apoptosis ==<br /> Apoptosis is one form of programmed cell death in multicellular organisms. There are <br /> multiple tags that are on a cell that signal for it to go to the apoptotic pathway. Once tagged, cells <br /> go through a biochemical pathway that changes the cells morphology and leads to the “suicide” <br /> or self death of the cell. A cell can go through either an extrinsic or an intrinsic pathway in order <br /> to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer <br /> lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell <br /> Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes <br /> Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing <br /> apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting <br /> old, it has degradation of its membranes. This degradation also leads to the release of <br /> Cytochrome C which would signal that the cell is old and ready to be killed off. Without <br /> Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would <br /> never be activated. Same as if there are mutations in cytochrome C causing it to be unable to <br /> permeate through the membrane, or if there is a mutation that increases the permeability of it <br /> through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C <br /> Proteopedia)<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3033616 2019-04-24T15:29:08Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Structure ==<br /> Cytochrome C is a heme protein (or a part of the heme family) which means that it has a <br /> heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to <br /> cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central <br /> iron atom. They can form different compounds by having different attachments around the 8 <br /> cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme <br /> form, the other axial position is usually left empty however, it can be occupied by other <br /> molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and <br /> allows for easier attachment. The other forms contain anywhere from one to seven methionine <br /> groups on what we perceive the left side of the heme group. When drawn out, the structure of <br /> Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior <br /> to adding side chains. The side chains which determine overall function are branched off of the <br /> central heme group and vary depending on the proteins location in the cell. They can have one <br /> form of side chain branching off at multiple locations, like a methionine attaching at multiple <br /> locations, or it can have different types of attachments, like one methionine at a location and then <br /> a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' )<br /> <br /> == Function ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3033614 2019-04-24T15:27:42Z

<p>Adis Hasic: </p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> Cytochrome C is a heme family protein that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a perfect beginner protein to experiment with. However simple, it is a very important protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day<br /> <br /> == Function ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic https://proteopedia.org/index.php?title=Cytochrome_C_-Adis&diff=3033605 2019-04-24T15:24:47Z

<p>Adis Hasic: New page: ==Cytochrome C== &lt;StructureSection load=&#039;1stp&#039; size=&#039;340&#039; side=&#039;right&#039; caption=&#039;Caption for this structure&#039; scene=&#039;&#039;&gt; This is a default text for your page &#039;&#039;&#039;Cytochrome C -Adis&#039;&#039;&#039;. Click a...</p> <hr /> <div>==Cytochrome C==<br /> &lt;StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''&gt;<br /> This is a default text for your page '''Cytochrome C -Adis'''. Click above on '''edit this page''' to modify. Be careful with the &amp;lt; and &amp;gt; signs.<br /> You may include any references to papers as in: the use of JSmol in Proteopedia &lt;ref&gt;DOI 10.1002/ijch.201300024&lt;/ref&gt; or to the article describing Jmol &lt;ref&gt;PMID:21638687&lt;/ref&gt; to the rescue.<br /> <br /> == Function ==<br /> <br /> == Disease ==<br /> <br /> == Relevance ==<br /> <br /> == Structural highlights ==<br /> <br /> This is a sample scene created with SAT to &lt;scene name=&quot;/12/3456/Sample/1&quot;&gt;color&lt;/scene&gt; by Group, and another to make &lt;scene name=&quot;/12/3456/Sample/2&quot;&gt;a transparent representation&lt;/scene&gt; of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.<br /> <br /> &lt;/StructureSection&gt;<br /> == References ==<br /> &lt;references/&gt;</div>

Adis Hasic