| Description | This entry consists of electron transfer proteins found as components of oxidoreductase enzymes in bacteria and archaea. So far, these proteins have been shown to be components of sulphite reductase, which catalyses the production of hydrogen sulphide from sulphite, dihydroorotate dehydrogenase involved in pyrimidine biosynthesis, and hydrogenase [ , , ]. Structural studies of the PyrK component of dihydroorotate dehydrogenase show that it contains a 2Fe-2S cluster, an FAD cofactor and an NAD(+) binding region, with a similar overall fold to other members of the NADPH-ferrodoxin superfamily []. Its role is to transfer electrons derived from oxidation of the physiological substrate, via the iron-sulphur cluster, to the FAD cofactor where the ultimate electron acceptor is reduced. | Name | Cytochrome-c3 hydrogenase, gamma subunit |
| Short Name | Cyt_c3_hydrogenase_gsu | Type | Family |
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