Flavocytochrome
From Proteopedia
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| - | * '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br /> | + | * '''Flavocytochrome c''' or '''flavocytochrome c sulphide dehydrogenase''' or '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br /> |
* '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref> | * '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref> | ||
| + | * '''Flavocytochrome b2''' is a L-lactate/cytochrome c oxidoreductase<ref>PMID:15260495</ref> | ||
| + | * '''Flavocytochrome b558''' is the catalytic component of the phagocyte NADPH oxidase | ||
| - | <scene name='44/442751/Cv/10'>Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid</scene> (PDB code [[2b7r]]). | + | <scene name='44/442751/Cv/10'>Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid</scene> (PDB code [[2b7r]]<ref>PMID:16699170</ref>). |
*<scene name='44/442751/Cv/12'>1st Heme binding site</scene>. Water molecules are shown as red spheres. | *<scene name='44/442751/Cv/12'>1st Heme binding site</scene>. Water molecules are shown as red spheres. | ||
*<scene name='44/442751/Cv/13'>1st Heme Fe coordination site</scene>. | *<scene name='44/442751/Cv/13'>1st Heme Fe coordination site</scene>. | ||
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Interestedly, that all 4 heme groups are <scene name='44/442751/Cv/20'>covalently bound with Cys residues</scene> in heme-containing flavocytochrome c3 (PDB code [[2b7r]]). | Interestedly, that all 4 heme groups are <scene name='44/442751/Cv/20'>covalently bound with Cys residues</scene> in heme-containing flavocytochrome c3 (PDB code [[2b7r]]). | ||
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| + | <scene name='44/442751/Cv/26'>All Fe of 4 heme groups are coordinated with His residues</scene>. | ||
<scene name='44/442751/Cv/22'>Fumaric acid binding site</scene>. | <scene name='44/442751/Cv/22'>Fumaric acid binding site</scene>. | ||
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<scene name='44/442751/Cv/25'>Na coordination site</scene>. | <scene name='44/442751/Cv/25'>Na coordination site</scene>. | ||
| - | </StructureSection> | ||
== 3D Structures of flavocytochrome == | == 3D Structures of flavocytochrome == | ||
| + | [[Flavocytochrome 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | **[[1wlp]] – Fc B558 - human | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK. Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry. 2002 Jul 9;41(27):8551-6. PMID:12093271
- ↑ Mowat CG, Wehenkel A, Green AJ, Walkinshaw MD, Reid GA, Chapman SK. Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of L-lactate dehydrogenation. Biochemistry. 2004 Jul 27;43(29):9519-26. PMID:15260495 doi:http://dx.doi.org/10.1021/bi049263m
- ↑ Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK. A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina. J Biol Chem. 2006 Jul 21;281(29):20589-97. Epub 2006 May 12. PMID:16699170 doi:http://dx.doi.org/10.1074/jbc.M603077200
