Cytochrome d
| 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 | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| 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, and cytochrome cd1 (NirS; SCOP b.70.2), a nitrite reductase.
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).