Entry |
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Name |
anaerobic carbon monoxide dehydrogenase;
Ni-CODH;
carbon-monoxide dehydrogenase (ferredoxin)
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Class |
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With an iron-sulfur protein as acceptor
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Sysname |
carbon-monoxide,water:ferredoxin oxidoreductase
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Reaction(IUBMB) |
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+ [RN: R07157]
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Reaction(KEGG) |
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Substrate |
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Product |
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Comment |
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.
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History |
EC 1.2.7.4 created 2003 (EC 1.2.99.2 created 1982, modified 1990, modified 2003, incorporated 2015), modified 2016
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Pathway |
ec00720 | Carbon fixation pathways in prokaryotes |
ec01120 | Microbial metabolism in diverse environments |
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Orthology |
K00192 | anaerobic carbon-monoxide dehydrogenase, CODH/ACS complex subunit alpha |
K00198 | anaerobic carbon-monoxide dehydrogenase catalytic subunit |
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Genes |
» show all
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Reference |
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Authors |
Ragsdale SW, Clark JE, Ljungdahl LG, Lundie LL, Drake HL. |
Title |
Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein. |
Journal |
J Biol Chem 258:2364-9 (1983) |
Reference |
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Authors |
Diekert G, Ritter M. |
Title |
Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum. |
Journal |
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Reference |
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Authors |
Bonam D, Ludden PW. |
Title |
Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum. |
Journal |
J Biol Chem 262:2980-7 (1987) |
Reference |
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Authors |
Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW. |
Title |
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. |
Journal |
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Sequence |
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Reference |
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Authors |
Dobbek H, Svetlitchnyi V, Gremer L, Huber R, Meyer O. |
Title |
Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. |
Journal |
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Sequence |
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Reference |
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Authors |
Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL |
Title |
A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. |
Journal |
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Sequence |
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Reference |
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Authors |
Can M, Armstrong FA, Ragsdale SW |
Title |
Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase. |
Journal |
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Other DBs |
ExplorEnz - The Enzyme Database: | 1.2.7.4 |
ExPASy - ENZYME nomenclature database: | 1.2.7.4 |
BRENDA, the Enzyme Database: | 1.2.7.4 |
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LinkDB |
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