| Ubiquinol oxidase (electrogenic, proton-motive force generating; Cytochrome bd) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Predicted structure of E. coli Cytochrome bd-1 | |||||||||
| Identifiers | |||||||||
| EC no. | 7.1.1.7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Cytochrome d, previously known as cytochrome a2, is a name for all cytochromes (electron-transporting heme proteins) that contain heme D as a cofactor. Two unrelated classes of cytochrome d are known: Cytochrome bd, an enzyme that generates a charge across the membrane so that protons will move,[1] and cytochrome cd1 (NirS; SCOP b.70.2), a nitrite reductase.[2]
Cytochrome bd is found in plenty of aerobic bacteria, especially when it has grown with a limited oxygen supply. Compared to other terminal oxidases, it is notable for its high oxygen affinity and resistance to cyanide poisoning. It has a group of very similar relatives that do not use heme D, known as cyanide insensitive oxidases (CIOs).[3]
- ^ EC 7.1.1.7
- ^ "Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Nomenclature of electron-transfer proteins. Recommendations 1989" (PDF). European Journal of Biochemistry. 200 (3): 599–611. September 1991. doi:10.1111/j.1432-1033.1991.tb16223.x. PMID 1655423.
- ^ Borisov VB, Gennis RB, Hemp J, Verkhovsky MI (November 2011). "The cytochrome bd respiratory oxygen reductases". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807 (11): 1398–413. doi:10.1016/j.bbabio.2011.06.016. PMC 3171616. PMID 21756872.