Flavocytochrome: Difference between revisions

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<StructureSection load='2b7r' size='350' side='right' caption='Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code [[2b7r]]).' scene='44/442751/Cv/9' >
<StructureSection load='2b7r' size='350' side='right' caption='Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code [[2b7r]]).' scene='' >




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


 
<scene name='44/442751/Cv/10'>Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid</scene> (PDB code [[2b7r]]).
</StructureSection>
</StructureSection>


Revision as of 12:12, 24 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).

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 24-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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