EC 1.2.7.4 - Anaerobic carbon-monoxide dehydrogenase

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IntEnz Enzyme Nomenclature
EC 1.2.7.4

Names

Accepted name:
anaerobic carbon-monoxide dehydrogenase
Other names:
Ni-CODH
carbon-monoxide dehydrogenase (ferredoxin)
Systematic name:
carbon-monoxide,water:ferredoxin oxidoreductase

Reaction

Cofactors

Comments:

This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [4Fe-4S] D-cluster; and two [4Fe-4S] B-clusters. In methanogenic archaea additional [4Fe-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic 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:0043885
UniProtKB/Swiss-Prot: (26) [show] [UniProt]

References

  1. Ragsdale, S.W., Clark, J.E., Ljungdahl, L.G., Lundie, L.L. and Drake, H.L.
    Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum a nickel, iron-sulfur protein.
    J. Biol. Chem. 258: 2364-2369 (1983). [PMID: 6687389]
  2. Diekert, G., Ritter, M.
    Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum.
    FEBS Lett. 151: 41-44 (1983). [PMID: 6687458]
  3. Bonam, D., Ludden, P. W.
    Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.
    J. Biol. Chem. 262: 2980-2987 (1987). [PMID: 3029096]
  4. Drennan, C. L., Heo, J., Sintchak, M. D., Schreiter, E., Ludden, P. W.
    Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.
    Proc. Natl. Acad. Sci. U.S.A. 98: 11973-11978 (2001). [PMID: 11593006]
  5. Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R., Meyer, O.
    Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.
    Science 293: 1281-1285 (2001). [PMID: 11509720]
  6. Doukov, T. I., Iverson, T. M., Seravalli, J., Ragsdale, S. W., Drennan, C. L.
    A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.
    Science 298: 567-572 (2002). [PMID: 12386327]
  7. Can, M., Armstrong, F. A., Ragsdale, S. W.
    Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase.
    Chem. Rev. 114: 4149-4174 (2014). [PMID: 24521136]

[EC 1.2.7.4 created 2003 (EC 1.2.99.2 created 1982, modified 1990, modified 2003, incorporated 2015), modified 2016]