EC 1.2.5.3 - Aerobic carbon monoxide dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.2.5.3

Names

Accepted name:
aerobic carbon monoxide dehydrogenase
Other names:
MoCu-CODH
coxSML (gene names)
molybdoenzyme carbon monoxide dehydrogenase
Systematic name:
carbon-monoxide:quinone oxidoreductase

Reaction

Cofactors

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008805
UniProtKB/Swiss-Prot:

References

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 Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli.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

[EC 1.2.5.3 created 2016]