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Literature summary extracted from

  • Stein, B.; Kirk, M.
    Orbital contributions to CO oxidation in Mo-Cu carbon monoxide dehydrogenase (2014), Chem. Commun. (Camb.), 50, 1104-1106.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.5.3 n-butylisocyanide
-
 Afipia carboxidovorans
1.2.5.3 n-butylisocyanide
-
 Hydrogenophaga pseudoflava

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.3 Cu
-
 Hydrogenophaga pseudoflava
1.2.5.3 Cu
-
 Afipia carboxidovorans
1.2.5.3 Mo
-
 Hydrogenophaga pseudoflava
1.2.5.3 Mo
-
 Afipia carboxidovorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.5.3 CO + a quinone + H2O Hydrogenophaga pseudoflava
-
 CO2 + a quinol
-
 ?
1.2.5.3 CO + a quinone + H2O Afipia carboxidovorans
-
 CO2 + a quinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.3 Afipia carboxidovorans P19920
-
-
1.2.5.3 Hydrogenophaga pseudoflava P19913 and P19914 and P19915 large, medium, and small subunit
-

Reaction

EC Number Reaction Comment Organism Reaction ID
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
a
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 Afipia carboxidovorans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.5.3 CO + a quinone + H2O
-
 Hydrogenophaga pseudoflava CO2 + a quinol
-
 ?
1.2.5.3 CO + a quinone + H2O
-
 Afipia carboxidovorans CO2 + a quinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.5.3 CODH
-
 Hydrogenophaga pseudoflava
1.2.5.3 CODH
-
 Afipia carboxidovorans
1.2.5.3 Mo-Cu carbon monoxide dehydrogenase
-
 Hydrogenophaga pseudoflava
1.2.5.3 Mo-Cu carbon monoxide dehydrogenase
-
 Afipia carboxidovorans
1.2.5.3 Mo/Cu CODH
-
 Hydrogenophaga pseudoflava
1.2.5.3 Mo/Cu CODH
-
 Afipia carboxidovorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.5.3 quinone
-
 Hydrogenophaga pseudoflava

General Information

EC Number General Information Comment 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 Afipia 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 Afipia carboxidovorans