Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With an iron-sulfur protein as acceptor
BRITE hierarchy

carbon-monoxide,water:ferredoxin oxidoreductase

CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+ [RN:R07157]

R07157;
(other) R08034 R09317
Reaction

CO [CPD:C00237];
H2O [CPD:C00001];
oxidized ferredoxin [CPD:C00139]

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.

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

1  [PMID:6687389]

Ragsdale SW, Clark JE, Ljungdahl LG, Lundie LL, Drake HL.

Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein.

J Biol Chem 258:2364-9 (1983)

2  [PMID:6687458]

Diekert G, Ritter M.

Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum.

FEBS Lett 151:41-4 (1983)
DOI:10.1016/0014-5793(83)80338-X

3  [PMID:3029096]

Bonam D, Ludden PW.

Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.

J Biol Chem 262:2980-7 (1987)

4  [PMID:11593006]

Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW.

Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.

Proc Natl Acad Sci U S A 98:11973-8 (2001)
DOI:10.1073/pnas.211429998

[rru:Rru_A1427]

5  [PMID:11509720]

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

Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.

Science 293:1281-5 (2001)
DOI:10.1126/science.1061500

[chy:CHY_0085]

6  [PMID:12386327]

Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL

A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase.

Science 298:567-72 (2002)
DOI:10.1126/science.1075843

[mta:Moth_1203]

7  [PMID:24521136]

Can M, Armstrong FA, Ragsdale SW

Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase.

Chem Rev 114:4149-74 (2014)
DOI:10.1021/cr400461p