BRENDA - Enzyme Database

Paramagnetic active site models for the molybdenum-copper carbon monoxide dehydrogenase

Gourlay, C.; Nielsen, D.; White, J.; Knottenbelt, S.; Kirk, M.; Young, C.; J. Am. Chem. Soc. 128, 2164-2165 (2006)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.5.3
Cu2+
-
Oligotropha carboxidovorans
1.2.5.3
Molybdenum
-
Oligotropha carboxidovorans
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.5.3
Oligotropha carboxidovorans
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.5.3
CO + a quinone + H2O
-
736301
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.5.3
molybdenum cofactor
presence of a square pyramidal (Mo) oxidized active site, i.e. [(MCD)MoVIOX(Fe-S)CuI(S-Cys)]n, MCD = molybdopterin cytosine dinucleotide, X = OH3 or O4, cofactor reaction mechanism, computational modelling, overview
Oligotropha carboxidovorans
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.5.3
molybdenum cofactor
presence of a square pyramidal (Mo) oxidized active site, i.e. [(MCD)MoVIOX(Fe-S)CuI(S-Cys)]n, MCD = molybdopterin cytosine dinucleotide, X = OH3 or O4, cofactor reaction mechanism, computational modelling, overview
Oligotropha carboxidovorans
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.5.3
Cu2+
-
Oligotropha carboxidovorans
1.2.5.3
Molybdenum
-
Oligotropha carboxidovorans
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.5.3
CO + a quinone + H2O
-
736301
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
1.2.5.3
additional information
the enzyme has a unique heterobimetallic Mo/Cu active site, mass spectrometric and EPR spectra analysis, overview. Key to the catalytic mechanism of the CODH site is the electronic communication between the Mo and Cu atoms
Oligotropha carboxidovorans
1.2.5.3
physiological function
the enzyme catalyzes the oxidation of CO to CO2, thereby providing carbon and energy to the organism and maintaining subtoxic levels of CO in the troposphere
Oligotropha carboxidovorans
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.5.3
additional information
the enzyme has a unique heterobimetallic Mo/Cu active site, mass spectrometric and EPR spectra analysis, overview. Key to the catalytic mechanism of the CODH site is the electronic communication between the Mo and Cu atoms
Oligotropha carboxidovorans
1.2.5.3
physiological function
the enzyme catalyzes the oxidation of CO to CO2, thereby providing carbon and energy to the organism and maintaining subtoxic levels of CO in the troposphere
Oligotropha carboxidovorans