Flavocytochrome: Difference between revisions

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<StructureSection load='2b7r' size='350' side='right' caption='Structure of heme-containing flavocytochrome c complex with FAD and fumaric acid (PDB code [[2b7r]]).' scene=''>
<StructureSection load='2b7r' size='400' side='right' caption='Structure of 6-aminohexanoate-dimer hydrolase complex with 6-aminohexanoate (PDB code [[2zm9]]).' scene=''>




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*  '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref>   
*  '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref>   


== Structural highlights ==
<scene name='44/442751/Cv/3'>The biological assembly of Yeast flavocytochrome b2 flavin-binding domain is homotetramer</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 13:34, 27 May 2018


  • Fcc catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.
  • Fcc3 has fumarate reductase activity[1]


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

Drag the structure with the mouse to rotate

3D Structures of flavocytochrome3D Structures of flavocytochrome

Updated on 27-May-2018

ReferencesReferences

  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

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Michal Harel, Alexander Berchansky, Joel L. Sussman