carbon-monoxide dehydrogenase (cytochrome b-561);
carbon monoxide oxidase;
carbon monoxide oxygenase (cytochrome b-561);
carbon monoxide:methylene blue oxidoreductase;
CO dehydrogenase;
carbon-monoxide dehydrogenase

Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With a cytochrome as acceptor

carbon monoxide,water:cytochrome b-561 oxidoreductase

CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561 [RN:R04698]

R04698;
(other) R00276

CO [CPD:C00237];
H2O [CPD:C00001];
ferricytochrome b-561 [CPD:C05305]

Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors.

1

Meyer, O., Jacobitz, S. and Kruger, B.

Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria.

FEMS Microbiol. Rev. 39 (1986) 161-179.

2  [PMID:2808305]

Jacobitz S, Meyer O.

Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities.

J. Bacteriol. 171 (1989) 6294-9.

Pseudomonas carboxydovorans

3  [PMID:7354006]

Meyer O, Schlegel HG.

Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans.

J. Bacteriol. 141 (1980) 74-80.

Pseudomonas carboxydovorans

4  [PMID:10430865]

Dobbek H, Gremer L, Meyer O, Huber R.

Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.

Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8884-9.

Oligotropha carboxidovorans

5  [PMID:10966817]

Hanzelmann P, Dobbek H, Gremer L, Huber R, Meyer O.

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 (2000) 1221-35.

Hydrogenophaga pseudoflava