Carbon-monoxide dehydrogenase (cytochrome b-561)

carbon-monoxide oxygenase
Identifiers
EC no.	1.2.2.4
CAS no.	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 / QuickGO
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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 (3): 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. doi:10.1128/jb.171.11.6294-6299.1989. PMC   210502 . PMID   2808305.
• Meyer O, Schlegel HG (1980). "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". J. Bacteriol. 141 (1): 74–80. doi:10.1128/jb.141.1.74-80.1980. 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 (16): 8884–9. Bibcode:1999PNAS...96.8884D. 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 (5): 1221–35. doi:10.1006/jmbi.2000.4023. PMID   10966817.