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.
carbon monoxide dehydrogenase, co dehydrogenase, co-dh, co dehydrogenase/acetyl-coa synthase, co dehydrogenase complex, ni-codh, codh ii, codh-ii, acetyl-coa synthase/carbon monoxide dehydrogenase, ni-containing carbon monoxide dehydrogenase, more
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SYSTEMATIC NAME
IUBMB Comments
carbon-monoxide,water:ferredoxin oxidoreductase
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.
competitive inhibitor of reduced CODHII with respect to the substrate CO, inhibition of dithionite- or Ti(III) citrate-reduced CODHII by potassium cyanide is fully reversible since the enzyme can be completely reactivated, sodium sulfide has no effect on the reactivation of cyanide-inhibited CODHII in the presence of dithionite
0.075 mM, reversible, competitive inhibition of reduced CODHII with respect to the substrate carbon monoxide, which protects reduced CODHII against inhibition by cyanide, inhibited CODHII regains initial activity after a 15-25-min incubation at 70°C with dithionite or Ti(III) citrate under CO or N2, while slower and partial reactivation to 30-50% of the initial activity occurs with dithiothreitol or without reductants
CooC proteins are ATPases involved in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenases