Flavocytochrome: Difference between revisions

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*<scene name='44/442751/Cv/14'>2nd Heme binding site</scene>.
*<scene name='44/442751/Cv/14'>2nd Heme binding site</scene>.
*<scene name='44/442751/Cv/15'>2nd Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/15'>2nd Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/16'>3rd Heme binding site</scene>.
*<scene name='44/442751/Cv/17'>3rd Heme Fe coordination site</scene>.
</StructureSection>
</StructureSection>



Revision as of 15:15, 25 March 2019


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

(PDB code 2b7r).

  • . Water molecules are shown as red spheres.
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Structure of heme-containing flavocytochrome c3 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 25-March-2019

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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