Flavocytochrome

From Proteopedia

Flavocytochrome c or flavocytochrome c sulphide dehydrogenase or Fcc catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c. Fcc3 has fumarate reductase activity[1] Flavocytochrome b2 is a L-lactate/cytochrome c oxidoreductase[2] Flavocytochrome b558 is the catalytic component of the phagocyte NADPH oxidase Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code 2b7r[3]). 1st Heme binding site. Water molecules are shown as red spheres. 1st Heme Fe coordination site. 2nd Heme binding site. 2nd Heme Fe coordination site. 3rd Heme binding site. 3rd Heme Fe coordination site. 4th Heme binding site. 4th Heme Fe coordination site. Interestedly, that all 4 heme groups are covalently bound with Cys residues in heme-containing flavocytochrome c3 (PDB code 2b7r). All Fe of 4 heme groups are coordinated with His residues. Fumaric acid binding site. FAD binding site. Na coordination site. 3D Structures of flavocytochrome Flavocytochrome 3D structures

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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