EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   1.2.5.3 | more |
air-stable CO dehydrogenase having a binuclear molybdenum- and copper-containing active site catalyzes the first step in this process, the oxidation of CO to CO2, with the reducing equivalents. Enzyme reduction and reactivity with H2, kinetics, overview |
Afipia carboxidovorans |
? |
- |
? |
| 1.2.5.3 | more |
carbon monoxide dehydrogenases (CO dehydrogenases) are enzymes which catalyze the oxidation of CO to CO2 yielding two electrons and two protons (CO + H2O = CO2 + 2e- + 2H+) or the reverse reaction. CO oxidation by CO dehydrogenase proceeds at a unique bimetallic [CuSMoO2] cluster which matures posttranslationally while integrated into the completely folded apoenzyme |
Afipia carboxidovorans |
? |
- |
? |
| 1.2.5.3 | more |
analysis of mechanism of H2 oxidation, which involves initial binding of H2 to the copper of the binuclear center, displacing the bound water, followed by sequential deprotonation through a copper-hydride intermediate to reduce the binuclear center.The enzyme can be reduced by H2 with a limiting rate constant of 5.3/s and a dissociation constant Kd of 0.525 mM, steady-state and stopped-flow rapid reaction kinetics, overview |
Afipia carboxidovorans |
? |
- |
? |
| 1.2.5.3 | more |
quinones are unusual physiological oxidants for this family of enzymes |
Afipia carboxidovorans |
? |
- |
? |
| 1.2.5.3 | more |
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site |
- |
? |
- |
? |
| 1.2.5.3 | more |
the CO dehydrogenation reaction requires the oxidized state of the enzyme. The oxidation of CO mediated by CO dehydrogenase is followed spectrophotometrically with 1-phenyl-2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride/1-methoxyphenazine methosulfate as artificial electron acceptors. Oxidation of xanthine by CO dehydrogenase |
Afipia carboxidovorans |
? |
- |
? |
| 1.2.5.3 | more |
is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons |
Afipia carboxidovorans |
? |
- |
- |
| 1.2.5.3 | more |
the CO dehydrogenation reaction requires the oxidized state of the enzyme. The oxidation of CO mediated by CO dehydrogenase is followed spectrophotometrically with 1-phenyl-2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride/1-methoxyphenazine methosulfate as artificial electron acceptors. Oxidation of xanthine by CO dehydrogenase |
Afipia carboxidovorans DSM 1227 |
? |
- |
? |
| 1.2.5.3 | more |
is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons |
Afipia carboxidovorans DSM 1227 |
? |
- |
- |
| 1.2.5.3 | more |
routine activity is determined by the CO-dependent reduction of methylene blue. No activity with cytochrome b561. Quinone substrates interacted with CODH at its FAD site |
Afipia carboxidovorans ATCC 49405 |
? |
- |
? |
