ExplorEnz: EC 1.2.5.3

Your query returned 1 entry. Printable version

1.2.5.3

Accepted name:

aerobic carbon monoxide dehydrogenase

Reaction:

CO + a quinone + H₂O = CO₂ + a quinol

Other name(s):

MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase

Systematic name:

carbon-monoxide,water:quinone oxidoreductase

Comments:

This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO₂ under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO₂ that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor [5]. cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Gremer, L., Kellner, S., Dobbek, H., Huber, R. and Meyer, O. Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli. J. Biol. Chem. 275 (2000) 1864–1872. [DOI] [PMID: 10636886]
2.	Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R. and Meyer, O. Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proc. Natl. Acad. Sci. USA 99 (2002) 15971–15976. [DOI] [PMID: 12475995]
3.	Gnida, M., Ferner, R., Gremer, L., Meyer, O. and Meyer-Klaucke, W. A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy. Biochemistry 42 (2003) 222–230. [DOI] [PMID: 12515558]
4.	Resch, M., Dobbek, H. and Meyer, O. Structural and functional reconstruction in situ of the [CuSMoO₂] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans. J. Biol. Inorg. Chem. 10 (2005) 518–528. [DOI] [PMID: 16091936]
5.	Wilcoxen, J., Zhang, B. and Hille, R. Reaction of the molybdenum- and copper-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans with quinones. Biochemistry 50 (2011) 1910–1916. [DOI] [PMID: 21275368]
6.	Pelzmann, A.M., Mickoleit, F. and Meyer, O. Insights into the posttranslational assembly of the Mo-, S- and Cu-containing cluster in the active site of CO dehydrogenase of Oligotropha carboxidovorans. J. Biol. Inorg. Chem. 19 (2014) 1399–1414. [DOI] [PMID: 25377894]
7.	Hille, R., Dingwall, S. and Wilcoxen, J. The aerobic CO dehydrogenase from Oligotropha carboxidovorans. J. Biol. Inorg. Chem. 20 (2015) 243–251. [DOI] [PMID: 25156151]

[EC 1.2.5.3 created 2016]