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Literature summary extracted from

  • Gourlay, C.; Nielsen, D.; White, J.; Knottenbelt, S.; Kirk, M.; Young, C.
    Paramagnetic active site models for the molybdenum-copper carbon monoxide dehydrogenase (2006), J. Am. Chem. Soc., 128, 2164-2165.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.5.3 Cu2+
-
 Afipia carboxidovorans
1.2.5.3 Molybdenum
-
 Afipia carboxidovorans

Organism

EC Number Organism UniProt Comment Textmining
1.2.5.3 Afipia carboxidovorans
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.2.5.3 CODH
-
 Afipia carboxidovorans
1.2.5.3 molybdenum-copper carbon monoxide dehydrogenase
-
 Afipia carboxidovorans

Cofactor

EC Number Cofactor Comment 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 Afipia carboxidovorans

General Information

EC Number General Information Comment 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 Afipia 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 Afipia carboxidovorans