This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a cytochrome as acceptor. The systematic name of this enzyme class is hydrogen:ferricytochrome-c3 oxidoreductase. Other names in common use include H2:ferricytochrome c3 oxidoreductase, cytochrome c3 reductase, cytochrome hydrogenase, and hydrogenase [ambiguous]. It has 3 cofactors: iron, Nickel, and Iron-sulfur.
The coenzyme Q : cytochrome c – oxidoreductase, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain, playing a critical role in biochemical generation of ATP. Complex III is a multisubunit transmembrane protein encoded by both the mitochondrial and the nuclear genomes. Complex III is present in the mitochondria of all animals and all aerobic eukaryotes and the inner membranes of most eubacteria. Mutations in Complex III cause exercise intolerance as well as multisystem disorders. The bc1 complex contains 11 subunits, 3 respiratory subunits, 2 core proteins and 6 low-molecular weight proteins.
A hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2), as shown below:
Cupriavidus necator is a Gram-negative soil bacterium of the class Betaproteobacteria.
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Hydrogenases are enzymes that catalyze the reversible activation of hydrogen and which occur widely in prokaryotes as well as in some eukaryotes. There are various types of hydrogenases, but all of them seem to contain at least one iron-sulphur cluster. They can be broadly divided into two groups: hydrogenases containing nickel and, in some cases, also selenium and those lacking nickel.
[NiFe] hydrogenase is a type of hydrogenase, which is an oxidative enzyme that reversibly converts molecular hydrogen in prokaryotes including Bacteria and Archaea. The catalytic site on the enzyme provides simple hydrogen-metabolizing microorganisms a redox mechanism by which to store and utilize energy via the reaction
References
DerVartanian DV; Le Gall J (1974). "A monomolecular electron transfer chain: structure and function of cytochrome c3". Biochim. Biophys. Acta. 346 (1): 79–99. doi:10.1016/0304-4173(74)90012-3. PMID4364940.
Higuchi Y, Yasuoka N, Kakudo M, Katsube Y, Yagi T, Inokuchi H (1987). "Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F". J. Biol. Chem. 262 (6): 2823–5. PMID3546297.
Rilkis E; Rittenberg D (1961). "Some observations on the enzyme, hydrogenase". J. Biol. Chem. 236: 2526–2529. PMID13741672.
Sadana JC; Morey AV (1961). "Purification and properties of the hydrogenase of Desulfovibrio desulfuricans". Biochim. Biophys. Acta. 50: 153–163. doi:10.1016/0006-3002(61)91072-1. PMID13745271.
Fontecilla-Camps JC; Charon, MH; Piras, C; Hatchikian, EC; Frey, M; Fontecilla-Camps, JC (1995). "Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas". Nature. 373 (6515): 580–7. Bibcode:1995Natur.373..580V. doi:10.1038/373580a0. PMID7854413. S2CID4335445.
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