Carbon-monoxide dehydrogenase (cytochrome b-561)
| carbon-monoxide oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.2.2.4 | ||||||||
| CAS number | 64972-88-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a carbon-monoxide dehydrogenase (cytochrome b-561) (EC 1.2.2.4) is an enzyme that catalyzes the chemical reaction
- CO + H2O + 2 ferricytochrome b-561 CO2 + 2 H+ + 2 ferrocytochrome b-561
The 3 substrates of this enzyme are CO, H2O, and ferricytochrome b-561, whereas its 3 products are CO2, H+, and ferrocytochrome b-561.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is carbon monoxide,water:cytochrome b-561 oxidoreductase. Other names in common use include carbon monoxide oxidase, carbon monoxide oxygenase (cytochrome b-561), carbon monoxide:methylene blue oxidoreductase, CO dehydrogenase, and carbon-monoxide dehydrogenase.
References
- Meyer O, Jacobitz S & Kruger B (1986). "Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria". FEMS Microbiol. Rev. 39: 161–179. doi:10.1111/j.1574-6968.1986.tb01858.x.
- Jacobitz S, Meyer O (1989). "Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities". J. Bacteriol. 171 (11): 6294–9. PMC 210502
. PMID 2808305. - Meyer O, Schlegel HG (1980). "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". J. Bacteriol. 141 (1): 74–80. PMC 293533. PMID 7354006.
- Dobbek H, Gremer L, Meyer O, Huber R (1999). "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine". Proc. Natl. Acad. Sci. U.S.A. 96: 8884–9. doi:10.1073/pnas.96.16.8884. PMC 17702. PMID 10430865.
- Hanzelmann P, Dobbek H, Gremer L, Huber R, Meyer O (2000). "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase". J. Mol. Biol. 301: 1221–35. doi:10.1006/jmbi.2000.4023. PMID 10966817.
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