In molecular biology, flavocytochrome c sulfide dehydrogenase is an enzyme found in sulfur-oxidising bacteria such as the purple phototrophicbacteriaChromatium vinosum.[1][2] These enzymes are dimers of a flavoprotein and a dihaem cytochrome that carry out hydrogen sulfide-dependent cytochrome Creduction. 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
^ abChen ZW, Koh M, Van Driessche G, Van Beeumen JJ, Bartsch RG, Meyer TE, Cusanovich MA, Mathews FS (October 1994). "The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium". Science. 266 (5184): 430–2. doi:10.1126/science.7939681. PMID7939681.
^Quentmeier A, Hellwig P, Bardischewsky F, Wichmann R, Friedrich CG (November 2004). "Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus". Biochemistry. 43 (46): 14696–703. doi:10.1021/bi048568y. PMID15544340.