Carbon-monoxide dehydrogenase (cytochrome b-561)

From Wikipedia, the free encyclopedia

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 $\rightleftharpoons$ 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.

[edit] References

IUBMB entry for 1.2.2.4
BRENDA references for 1.2.2.4 (Recommended.)
PubMed references for 1.2.2.4
PubMed Central references for 1.2.2.4
Google Scholar references for 1.2.2.4
Meyer O, Jacobitz S and Kruger B (1986). "Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria". FEMS Microbiol. Rev. 39: 161–179.
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: 6294–9. PMID 2808305.
Meyer O, Schlegel HG (1980). "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". J. Bacteriol. 141: 74–80. 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. 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.