Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3
carbon-monoxide dehydrogenase (acceptor)
carbon-monoxide:(acceptor) oxidoreductase
CYS 42;CYS 47;CYS 50;CYS 62(2Fe-2S cluster-1 binding)
CYS 102;CYS 105;CYS 137;CYS 139(2Fe-2S cluster-2 binding)
CYS 388(Copper binding);GLU 763(Molybdenum binding)
EYS 388(Copper binding);GLU 763(Molybdenum binding)
Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine.
The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase.
Binding of flavin adenine dinucleotide to molybdenum-containing carbon monoxide dehydrogenase from Oligotropha carboxidovorans. Structural and functional analysis of a carbon monoxide dehydrogenase species in which the native flavoprotein has been replaced by its recombinant counterpart produced in Escherichia coli.
The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy.
Quantum chemical modeling of CO oxidation by the active site of molybdenum CO dehydrogenase.
Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans.
This enzyme is composed of large subunits with dinuclear cluster of Mo and Cu along with Molybdopterin cytosine dinucleotide(MCD) as cofactors, small subunits with two iron-sulfur clusters, and medium subunits with FAD as cofactor. Ni-containing carbon monoxide dehydrogenases and bifunctional enzymes (with acetyl-CoA synthetase) are not homologous, which classified into the identical E.C. According to the literature [3], this enzyme catalyzes the following reactions: (A) Oxidation of CO with H2O, yielding CO2, two electrons and two protons (H+) ions: (B) Electron transfer from CO to S-selanylcysteine 388 (EYS 388 of 1qj2): (C) Electron transfer from S-selanylcysteine 388 (EYS 388 of 1qj2) to Molybdenum cofactor: (D) Electron transfer from Molybdenum cofactor to MCD cofactor: (E) Electron transfer from MCD cofactor to 2Fe-2S cluster-2: (F) Electron transfer from 2Fe-2S cluster-2 to 2Fe-2S cluster-1: (G) Electron transfer from 2Fe-2S cluster-1 to flavin group of FAD: (H) Electron transfer from flavin group of FAD to electron acceptor protein: