IUBMB Enzyme Nomenclature

EC 1.2.2.4

Accepted name: carbon-monoxide dehydrogenase (cytochrome b-561)

Reaction: CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561

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

Systematic name: carbon monoxide,water:cytochrome b-561 oxidoreductase

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

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, CAS registry number: 395639-79-9

References:

1. Meyer, O., Jacobitz, S. and Krüger, B. Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria. FEMS Microbiol. Rev. 39 (1986) 161-179.

2. Jacobitz, S. and 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) 6294-6299. [PMID: 2808305]

3. Meyer, O. and Schlegel, H.-G. Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans. J. Bacteriol. 141 (1980) 74-80. [PMID: 7354006]

4. Dobbek, H., Gremer, L., Meyer, O. and Huber, R. Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proc. Natl. Acad. Sci. USA 96 (1999) 8884-8889. [PMID: 10430865]

5. Hänzelmann, P., Dobbek, H., Gremer, L., Huber, R. and 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) 1221-1235. [PMID: 10966817]

[EC 1.2.2.4 created 1999 (EC 1.2.3.10 created 1990, incorporated 2003), modified 2003]


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