BRENDA - Enzyme Database

Orbital contributions to CO oxidation in Mo-Cu carbon monoxide dehydrogenase

Stein, B.; Kirk, M.; Chem. Commun. (Camb.) 50, 1104-1106 (2014)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.5.3
n-butylisocyanide
-
Hydrogenophaga pseudoflava
1.2.5.3
n-butylisocyanide
-
Oligotropha carboxidovorans
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.5.3
Cu
-
Hydrogenophaga pseudoflava
1.2.5.3
Cu
-
Oligotropha carboxidovorans
1.2.5.3
Mo
-
Hydrogenophaga pseudoflava
1.2.5.3
Mo
-
Oligotropha carboxidovorans
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.5.3
CO + a quinone + H2O
Hydrogenophaga pseudoflava
-
CO2 + a quinol
-
-
?
1.2.5.3
CO + a quinone + H2O
Oligotropha carboxidovorans
-
CO2 + a quinol
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.5.3
Hydrogenophaga pseudoflava
P19913 and P19914 and P19915
large, medium, and small subunit
-
1.2.5.3
Oligotropha carboxidovorans
P19920
-
-
Reaction
EC Number
Reaction
Commentary
Organism
1.2.5.3
CO + a quinone + H2O = CO2 + a quinol
reaction mechanism that initially involves nucleophilic attack of a Mo=O oxo on the carbon center of Cu(I)-CO, resulting in a 5-membered cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I that can bind HO-/H2O to yield 1-OH. This is followed by a second nucleophilic attack on the activated mu2-nu2 CO2 carbon centre of 1-OH to yield a Mo(IV)-bicarbonate product complex, 1-P. This second nucleophilic attack is suggested based on electronic structure description of cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I, which possesses a bent and activated CO2 bound to the Mo and Cu ions. Proposed catalytic cycle for CODH that avoids formation of a stable C-S bonded cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex II
Hydrogenophaga pseudoflava
1.2.5.3
CO + a quinone + H2O = CO2 + a quinol
reaction mechanism that initially involves nucleophilic attack of a Mo=O oxo on the carbon center of Cu(I)-CO, resulting in a 5-membered cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I that can bind HO-/H2O to yield 1-OH. This is followed by a second nucleophilic attack on the activated mu2-nu2 CO2 carbon centre of 1-OH to yield a Mo(IV)-bicarbonate product complex, 1-P. This second nucleophilic attack is suggested based on our electronic structure description of cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex I, which possesses a bent and activated CO2 bound to the Mo and Cu ions. Proposed catalytic cycle for CODH that avoids formation of a stable C-S bonded cyclic m2-e(2) CO2-bridged Mo(VI)-Cu(I)-Cys complex II
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
-
735935
Hydrogenophaga pseudoflava
CO2 + a quinol
-
-
-
?
1.2.5.3
CO + a quinone + H2O
-
735935
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.5.3
quinone
-
Hydrogenophaga pseudoflava
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.5.3
quinone
-
Hydrogenophaga pseudoflava
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.5.3
n-butylisocyanide
-
Hydrogenophaga pseudoflava
1.2.5.3
n-butylisocyanide
-
Oligotropha carboxidovorans
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.2.5.3
Cu
-
Hydrogenophaga pseudoflava
1.2.5.3
Cu
-
Oligotropha carboxidovorans
1.2.5.3
Mo
-
Hydrogenophaga pseudoflava
1.2.5.3
Mo
-
Oligotropha carboxidovorans
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.5.3
CO + a quinone + H2O
Hydrogenophaga pseudoflava
-
CO2 + a quinol
-
-
?
1.2.5.3
CO + a quinone + H2O
Oligotropha carboxidovorans
-
CO2 + a quinol
-
-
?
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
-
735935
Hydrogenophaga pseudoflava
CO2 + a quinol
-
-
-
?
1.2.5.3
CO + a quinone + H2O
-
735935
Oligotropha carboxidovorans
CO2 + a quinol
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
1.2.5.3
evolution
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde
Hydrogenophaga pseudoflava
1.2.5.3
evolution
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde substrates
Oligotropha carboxidovorans
1.2.5.3
additional information
mechanism of Mo/Cu carbon monoxide dehydrogenase, electronic structure contributions to reactivity, overview
Hydrogenophaga pseudoflava
1.2.5.3
additional information
mechanism of Mo/Cu carbon monoxide dehydrogenase, electronic structure contributions to reactivity, overview
Oligotropha carboxidovorans
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.2.5.3
evolution
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde
Hydrogenophaga pseudoflava
1.2.5.3
evolution
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde substrates
Oligotropha carboxidovorans
1.2.5.3
additional information
mechanism of Mo/Cu carbon monoxide dehydrogenase, electronic structure contributions to reactivity, overview
Hydrogenophaga pseudoflava
1.2.5.3
additional information
mechanism of Mo/Cu carbon monoxide dehydrogenase, electronic structure contributions to reactivity, overview
Oligotropha carboxidovorans