Sandbox Reserved 335: Difference between revisions

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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 <scene name='Sandbox_Reserved_335/Motif/1'>CXXCH motif</scene>, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/3'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />

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 <scene name='Sandbox_Reserved_335/Motif/2'>CXXCH motif</scene>, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/3'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />

In ''Rm''cyt''c'', the porphyrin ring is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>

In ''Rm''cyt''c'', the porphyrin ring is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/4'>His49 and Met100</scene>

Monoheme cytochromes ''c'' are involved in electron transport chains in both prokaryotes and eukaryotic mitochondria.<ref name=main /> They mediate the transfer of electrons mainly from the ''bc''1 complexes, or their analogs, in the [http://en.wikipedia.org/wiki/Electron_transport_chain electron transport chain] to heme-copper oxygen reductases (HCOs) during [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''3 oxygen reductases<ref name=main /><ref>PMID:14691678</ref>; these enzymes are membrane-bound and catalyze the reduction of O2 to water.<ref>PMID:11334784</ref> In addition to being involved in the electron transport systems 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].<ref name=main />

Sandbox Reserved 335: Difference between revisions

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@@ Line 22: / Line 22: @@
 <Structure load='3cp5' size='300' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_335/Heme/1' />
-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 <scene name='Sandbox_Reserved_335/Motif/1'>CXXCH motif</scene>, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/3'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />
+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 <scene name='Sandbox_Reserved_335/Motif/2'>CXXCH motif</scene>, where a histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> The other axial position, in monoheme cytochromes ''c'', may be left vacant or be occupied by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.<ref name=main />. The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/3'>A, C, and E</scene>. In ''Rm''cyt''c'' there are seven α-helices that are folded around the porphyrin ring, all connected by random coils.<ref name=main />
-In ''Rm''cyt''c'', the porphyrin ring is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/3'>His49 and Met100</scene>
+In ''Rm''cyt''c'', the porphyrin ring is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/4'>His49 and Met100</scene>
 Monoheme cytochromes ''c'' are involved in electron transport chains in both prokaryotes and eukaryotic mitochondria.<ref name=main /> They mediate the transfer of electrons mainly from the ''bc''<sub>1</sub> complexes, or their analogs, in the [http://en.wikipedia.org/wiki/Electron_transport_chain electron transport chain] to heme-copper oxygen reductases (HCOs) during [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''<sub>3</sub> oxygen reductases<ref name=main /><ref>PMID:14691678</ref>; these enzymes are membrane-bound and catalyze the reduction of O<sub>2</sub> to water.<ref>PMID:11334784</ref> In addition to being involved in the electron transport systems 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].<ref name=main />