Menaquinol oxidase (H+-transporting)
| Menaquinol oxidase (H+-transporting) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.10.3.12 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Menaquinol oxidase (H+-transporting) (EC 1.10.3.12, cytochrome aa3-600 oxidase, cytochrome bd oxidase) is an enzyme with systematic name menaquinol:O2 oxidoreductase (H+-transporting).[1][2][3] This enzyme catalyses the following chemical reaction
- 2 menaquinol + O2 2 menaquinone + 2 H2O
Cytochrome aa3-600, one of the respiratory oxidases from Bacillus subtilis, is a member of the heme-copper family of oxygen reductases.
References
- ↑ Lauraeus, M.; Wikstrom, M. (1993). "The terminal quinol oxidases of Bacillus subtilis have different energy conservation properties". J. Biol. Chem. 268 (15): 11470–11473. PMID 8388393.
- ↑ Lemma, E.; Simon, J.; Schagger, H.; Kroger, A. (1995). "Properties of the menaquinol oxidase (Qox) and of qox deletion mutants of Bacillus subtilis". Arch. Microbiol. 163 (6): 432–438. doi:10.1007/bf00272132. PMID 7575098.
- ↑ Yi, S.M.; Narasimhulu, K.V.; Samoilova, R.I.; Gennis, R.B.; Dikanov, S.A. (2010). "Characterization of the semiquinone radical stabilized by the cytochrome aa3-600 menaquinol oxidase of Bacillus subtilis". J. Biol. Chem. 285 (24): 18241–18251. doi:10.1074/jbc.M110.116186. PMC 2883873
. PMID 20351111.
External links
- Menaquinol oxidase (H -transporting) at the US National Library of Medicine Medical Subject Headings (MeSH)
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