Flavocytochrome c sulfide dehydrogenase
| Flavocytochrome c sulfide dehydrogenase, flavin-binding | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:PDB 1fcd EBI.jpg
the structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium chromatium vinosum at 2.5 angstroms resolution
|
|||||||||
| Identifiers | |||||||||
| Symbol | FCSD-flav_bind | ||||||||
| Pfam | PF09242 | ||||||||
| InterPro | IPR015323 | ||||||||
| SCOP | 1fcd | ||||||||
| SUPERFAMILY | 1fcd | ||||||||
|
|||||||||
In molecular biology, flavocytochrome c sulfide dehydrogenase is an enzyme found in sulfur-oxidising bacteria such as the purple phototrophic bacteria Chromatium vinosum.[1][2] These enzymes are dimers of a flavoprotein and a dihaem cytochrome that carry out hydrogen sulfide-dependent cytochrome C reduction. The dihaem cytochrome folds into two domains, each of which resembles mitochondrial cytochrome c, with the two haem groups bound to the interior of the subunit. The flavoprotein subunit has a glutathione reductase-like fold consisting of a beta(3,4)-alpha(3) core, and an alpha+beta sandwich. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. The flavoprotein contains a C-terminal domain required for binding to flavin, and subsequent electron transfer.[1] Electrons are transferred from the flavin to one of the haem groups in the cytochrome.
References
This article incorporates text from the public domain Pfam and InterPro IPR015323
