Flavocytochrome: Difference between revisions

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<scene name='44/442751/Cv/5'>Fe coordination site</scene>.
<scene name='44/442751/Cv/5'>Fe coordination site</scene>.
<scene name='44/442751/Cv/7'>Heme binding site</scene>.
</StructureSection>
</StructureSection>



Revision as of 15:46, 21 February 2016


  • Flavocytochrome b2 (Fcb2) is a flavin-dependent hydroxy acid dehydrogenase[1]

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  • FP450 BM3 is a fatty acid hydroxtylase from Bacillus megaterium[2]

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  • Fcc catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.
  • Fcc3 has fumarate reductase activity[3]

Structural highlights

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Yeast flavocytochrome b2 flavin-binding domain complex with FMN, MPD, phosphate, pyruvic acid (PDB code 1kbi)

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3D Structures of flavocytochrome3D Structures of flavocytochrome

Updated on 21-February-2016

ReferencesReferences

  1. Gondry M, Dubois J, Terrier M, Lederer F. The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins. Eur J Biochem. 2001 Sep;268(18):4918-27. PMID:11559361
  2. Ost TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S. Oxygen activation and electron transfer in flavocytochrome P450 BM3. J Am Chem Soc. 2003 Dec 10;125(49):15010-20. PMID:14653735 doi:http://dx.doi.org/10.1021/ja035731o
  3. 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

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