Proteopedia - User contributions [en]

Sulfite Oxidase

2009-04-15T20:45:03Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

<applet load='1sox' size='300' frame='true' align='right' caption='Insert caption here' />

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite, one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
<ref group='xtra'>PMID: 18583608</ref><ref group='xtra'>PMID: 17459792</ref><references group='xtra'/>

[[http://www.chem.arizona.edu/enemark/new/ Enemark Research Group]]

Sulfite Oxidase

2009-04-15T20:43:00Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite, one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />
<applet load='1sox' size='300' frame='true' align='right' caption='Insert caption here' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
<ref group='xtra'>PMID: 18583608</ref><ref group='xtra'>PMID: 17459792</ref><references group='xtra'/>

[[http://www.chem.arizona.edu/enemark/new/ Enemark Research Group]]

Sulfite Oxidase

2009-04-15T20:19:44Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite, one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
<ref group='xtra'>PMID: 18583608</ref><ref group='xtra'>PMID: 17459792</ref><references group='xtra'/>

[[http://www.chem.arizona.edu/enemark/new/ Enemark Research Group]]

Sulfite Oxidase

2009-04-15T20:14:32Z

Kimberly Meyers:

<applet load='1sox' size='300' frame='true' align='right' caption='Insert caption here' />

Blah blah.

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite, one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
<ref group='xtra'>PMID: 18583608</ref><ref group='xtra'>PMID: 17459792</ref><references group='xtra'/>

[[http://www.chem.arizona.edu/enemark/new/ Enemark Research Group]]

Sulfite Oxidase

2009-04-15T20:12:43Z

Kimberly Meyers:

== Tryptophan ==

Blah blah.

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite, one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
<ref group='xtra'>PMID: 18583608</ref><ref group='xtra'>PMID: 17459792</ref><references group='xtra'/>

[[http://www.chem.arizona.edu/enemark/new/ Enemark Research Group]]

Sulfite Oxidase

2009-04-15T19:54:06Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite, one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
<ref group='xtra'>PMID: 18583608</ref><ref group='xtra'>PMID: 17459792</ref><references group='xtra'/>

[[http://www.chem.arizona.edu/enemark/new/ Enemark Research Group]]

Sulfite Oxidase

2009-04-15T05:03:17Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

== Tryptophan's Importance in Sulfite Oxidase ==

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

== References ==
Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.

Feng C, Tollin G, Enemark JH. Biochim Biophys Acta. 2007. 1774(5), 527-539.

[[http://www.chem.arizona.edu/enemark/new/]]

Sulfite Oxidase

2009-04-15T04:25:55Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

----
Sulfite Oxidase Active Site: Tryptophan's Importance

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

[[Image:Sulfite-oxidase-active-site-500w.jpg]]

File:Sulfite-oxidase-active-site-500w.jpg

2009-04-15T04:25:02Z

Kimberly Meyers:

Sulfite Oxidase

2009-04-15T04:23:03Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Chicken Sulfite Oxidase' />

----
Sulfite Oxidase Active Site: Tryptophan's Importance

Tryptophan has been shown as a crucial amino acid that can facilitate electron transfer. A paper written by Shih C (Shih C, Museth AK, Abrahamsson M, Blanco-Rodriguez AM, Di Bilio AJ, Sudhamsu J, Crane BR, Ronayne KL, Towrie M, Vlcek A Jr, Richards JH, Winkler JR, Gray HB. Science. 2008. 320, 1760-1762.) suggests that multi-step electron tunneling can enhance charge transfer rates, in which redox active amino acid side chains act as intermediate donors or acceptors.

Since tryptophan is found in the active site of sulfite oxidase it is hypothesized that it plays a major role in the electron transfer rate of the enzyme. Currently, mutations of the tryptophan are being performed to see the effects that mutating the tryptophan with another amino acid, such as phenylalanine, will have on sulfite oxidase's electron transfer rate.

Sulfite Oxidase

2009-04-14T22:47:02Z

Kimberly Meyers:

Sulfite Oxidase

2009-04-14T22:46:09Z

Kimberly Meyers:

== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='2A99' size='300' frame='true' align='right' caption='Insert caption here' />

Sulfite Oxidase

2009-04-14T22:42:01Z

Kimberly Meyers:

<applet load='2A99' size='300' frame='true' align='right' caption='Insert caption here' />[[Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Sulfite Oxidase

2009-04-14T20:41:35Z

Kimberly Meyers:

Sulfite Oxidase

2009-04-14T20:41:13Z

Kimberly Meyers:

[[Image:Image:Chicken-sulfite-oxidase-500w.jpg]]
== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Sulfite Oxidase

2009-04-14T20:40:07Z

Kimberly Meyers:

== Sulfite Oxidase Background Information==

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

==Sulfite Oxidase Electron Transfer==

[[Image:Sulfite Oxidase electron transfer image.jpg]]

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite. One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
<applet load='Image:Chicken-sulfite-oxidase-500w.jpg' size='300' frame='true' align='right' caption='Insert caption here' />

Sulfite Oxidase

2009-04-14T20:29:48Z

Kimberly Meyers:

Sulfite Oxidase

2009-04-14T20:27:44Z

Kimberly Meyers:

Sulfite Oxidase

2009-04-14T20:24:25Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
--[[User:Kimberly Meyers|Kimberly Meyers]] 23:21, 14 April 2009 (IDT)

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite (Figure 1). One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.
[[Image:Sulfite Oxidase electron transfer image.jpg]]

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

Sulfite Oxidase

2009-04-14T20:21:39Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
--[[User:Kimberly Meyers|Kimberly Meyers]] 23:21, 14 April 2009 (IDT)

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite (Figure 1). One oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

Sulfite Oxidase

2009-04-14T20:19:17Z

Kimberly Meyers:

[[Image:Chicken-sulfite-oxidase-500w.jpg]]
Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite (Figure 1),[[Image:http://www.chem.arizona.edu/enemark/new/images/sulfite-oxidase-proposed-mechanism-500w.jpg] one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

Sulfite Oxidase

2009-04-14T20:16:53Z

Kimberly Meyers:

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite (Figure 1),[[Image:http://www.chem.arizona.edu/enemark/new/images/sulfite-oxidase-proposed-mechanism-500w.jpg] one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.
<applet load='Insert PDB code/Users/Kimberly/Pictures/chicken-sulfite-oxidase-500w.jpg' size='300' frame='true' align='right' caption='Insert caption here' />

Sulfite Oxidase

2009-04-14T20:14:36Z

Kimberly Meyers:

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite (Figure 1),[[Image:http://www.chem.arizona.edu/enemark/new/images/sulfite-oxidase-proposed-mechanism-500w.jpg] one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.
<applet load='http://www.chem.arizona.edu/enemark/new/images/chicken-sulfite-oxidase-500w.jpg' size='300' frame='true' align='right' caption='Insert caption here' />

Sulfite Oxidase

2009-04-14T20:00:51Z

Kimberly Meyers:

Sulfite Oxidase

2009-04-14T19:51:41Z

Kimberly Meyers:

Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, kidneys and livers. Very little can be seen in the brain, skeletal muscle, blood and spleen.

The enzyme is a homodimer, a chemical entity consisting of two identical subunits called monomers, which are linked together by intramolecular forces. Sulfite oxidase contains two identical subunits. Each subunit has two domains, iron and molybdenum that are linked together by a loop composed of amino acids.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site.

The molybdopertin cofactor is crucial to the enzyme because the oxidation of the sulfite occurs at the molybdenum center; the molybdenum center serves as the active site. When the molybdenum reacts with sulfite (Figure 1), one oxygen atom is transferred to sulfite, which produces sulfate and consequently reduces the molybdenum center by two electrons, thus resulting in Mo(IV). Intramolcular electron transfer from Mo(IV) to Fe(III) results in Fe(II) and Mo(V). One-electron photochemical reduction then moves Fe(II) to the exterior cytochrome resulting in Fe(III). This process occurs twice, and restores the enzyme to its original state.

Point mutations in sulfite oxidase and defects in the molybdenum cofactor synthesis can ultimately lead to sulfite oxidase deficiency. The disorder causes neurological disorders, mental retardation, physical deformities, deterioration of the brain, and ultimately death.

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Sulfite Oxidase

2009-04-13T19:40:06Z

Kimberly Meyers: Removing all content from page

Sulfite Oxidase

2009-04-13T19:39:17Z

Kimberly Meyers: New page: Sulfite oxidase is a crucial enzyme that is responsible for oxidizing harmful sulfites to sulfates. The enzyme is found in the mitochondria of the cell and mostly can be found in hearts, k...