| Type: | Domain | Name: | Cytochrome c-552/DMSO reductase-like, haem-binding domain |
| Description: | This entry represents a haem-binding domain found in cytochromes b558/566 (subunit A), c-551 and c-552, as well as in members of the type-II members of the microbial dimethyl sulphoxide (DMSO) reductase family.The DMSO reductase family is a large and rapidly expanding group of enzymes found in bacteria and archaea that share a common form of molybdenum cofactor known as bis(molybdopterin guanine dinucleotide)Mo []. In addition to the molybdopterin subunit, these enzymes also contain an iron-sulphur subunit. These include two distinct but very closely related periplasmic proteins of anaerobic respiration: selenate reductase and chlorate reductase []. Other proteins containing this subunit include dimethyl sulphide dehydrogenase and ethylbenzene dehydrogenase [, , ].One member of the DMSO reductase family is eythylbenzene dehydrogenase, which is a heterotrimer of three subunits that catalyses the anaerobic degradation of hydrocarbons (alpha, beta and gamma subunits). This entry matches the gamma subunit, whose structure is known []. The alpha subunit contains the catalytic centre as a Molybdenum cofactor-complex. This removes an electron-pair from the hydrocarbon and passes it along an electron transport system involving iron-sulphur complexes held in the beta subunit and a Haem b molecule contained in the gamma subunit. The electron-pair is then subsequently passed to an as yet unknown receiver. The enzyme is found in a variety of different bacteria. | Short Name: | Cyt-c552/DMSO_Rdtase_haem-bd |
