Flavocytochrome

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<StructureSection load='2b7r' size='450' side='right' caption='Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code [[2b7r]]).' scene='' >
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{{STRUCTURE_1kbi| PDB=1kbi | SIZE=400| SCENE=Flavocytochrome/Cv/1 |right|CAPTION=Yeast flavocytochrome b2 flavin-binding domain dimer complex with FMN, MPD, phosphate, pyruvic acid [[1kbi]] }}
 
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'''Flavocytochrome b2''' (Fcb2) is a flavin-dependent hydroxy acid dehydrogenase. FP450 BM3 is a fatty acid hydroxtylase from ''Bacillus'' ''megaterium''. Fcc catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c. Fcc3 has fumarate reductase activity.
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* '''Flavocytochrome c''' or '''flavocytochrome c sulphide dehydrogenase''' or '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br />
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* '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref>
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* '''Flavocytochrome b2''' is a L-lactate/cytochrome c oxidoreductase<ref>PMID:15260495</ref>
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* '''Flavocytochrome b558''' is the catalytic component of the phagocyte NADPH oxidase
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== 3D Structures of flavocytochrome ==
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<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>).
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*<scene name='44/442751/Cv/12'>1st Heme binding site</scene>. Water molecules are shown as red spheres.
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*<scene name='44/442751/Cv/13'>1st Heme Fe coordination site</scene>.
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*<scene name='44/442751/Cv/14'>2nd Heme binding site</scene>.
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*<scene name='44/442751/Cv/15'>2nd Heme Fe coordination site</scene>.
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*<scene name='44/442751/Cv/16'>3rd Heme binding site</scene>.
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*<scene name='44/442751/Cv/17'>3rd Heme Fe coordination site</scene>.
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*<scene name='44/442751/Cv/18'>4th Heme binding site</scene>.
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*<scene name='44/442751/Cv/19'>4th Heme Fe coordination site</scene>.
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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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]]).
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===FP450===
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<scene name='44/442751/Cv/26'>All Fe of 4 heme groups are coordinated with His residues</scene>.
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[[3kx3]], [[3kx4]], [[3kx5]], [[3ekb]], [[3ekd]], [[3ekf]], [[3nnb]], [[2yqo]], [[2yqp]], [[1p0v]], [[1p0w]], [[1p0x]], [[1jme]] – BmFP450 BM3 (mutant) – ''Bacillus megaterium''<br />
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<scene name='44/442751/Cv/22'>Fumaric acid binding site</scene>.
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[[2ij2]] - BmFP450 BM3<br />
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[[2uwh]] - BmFP450 BM3 (mutant)+palmitic acid<br />
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[[2j1m]], [[2j4s]] - BmFP450 BM3 + DMSO<br />
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[[3ben]] - BmFP450 BM3 heme domain+inhibitor<br />
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[[3vrd]] – Fc heme and FMN binding domains – ''Thermochromatium tepidum''
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===Fcb2===
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<scene name='44/442751/Cv/24'>FAD binding site</scene>.
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[[3ks0]] – mFcb2 heme domain+fragment antigen binding B2B4+Cyt b2 – mouse<br />
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<scene name='44/442751/Cv/25'>Na coordination site</scene>.
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[[2oz0]], [[1qcw]] – yFcb2 (mutant) – yeast<br />
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[[1kbi]], [[1fcb]] – yFcb2<br />
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[[1kbj]] – yFcb2 FMN binding domain<br />
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[[1sze]] – yFcb2 (mutant)+benzoylformate<br />
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[[1szf]], [[1lco]], [[1ldc]] – yFcb2 (mutant)+pyruvate derivative<br />
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[[1szg]] – yFcb2 (mutant)+sulfite<br />
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[[1ltd]] – yFcb2 +sulfite
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===Fcc===
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== 3D Structures of flavocytochrome ==
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[[Flavocytochrome 3D structures]]
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[[2b7r]], [[2b7s]], [[1q9i]], [[1p2e]], [[1p2h]], [[1lj1]], [[1m64]], [[1kss]], [[1ksu]], [[1jrx]], [[1jry]], [[1jrz]], [[1e39]] – SfFcc3 (mutant) – ''Shewanella frigidimarina''<br />
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</StructureSection>
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[[1qo8]], [[1qjd]] - SfFcc3<br />
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[[1y0p]] – SfFcc3+mesaconate<br />
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[[1wve]] – Fcc+4-cresol dehydrogenase – ''Pseudomonas putida''
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[[1wlp]] – Fc B-245 light chain - human
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code 2b7r).

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

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