Standard Article

CO Dehydrogenase

Part 5. Molybdenum/Tungsten

  1. Holger Dobbek1,
  2. Lothar Gremer2,
  3. Ortwin Meyer2,
  4. Robert Huber1

Published Online: 15 APR 2006

DOI: 10.1002/0470028637.met183

Handbook of Metalloproteins

Handbook of Metalloproteins

How to Cite

Dobbek, H., Gremer, L., Meyer, O. and Huber, R. 2006. CO Dehydrogenase. Handbook of Metalloproteins. 5.

Author Information

  1. 1

    Max-Planck-Institut für Biochemie, Martinsried bei München, Germany

  2. 2

    Universität Bayreuth, Bayreuth, Germany

Publication History

  1. Published Online: 15 APR 2006


Two principal types of CO dehydrogenases have been discovered, which are distinguished by their metal contents, amino acid sequences, molecular masses, and their sensitivity toward dioxygen.

The CODH from the aerobic eubacterium Oligotropha carboxidovorans catalyzes the oxidation of CO with H2O, yielding CO2, two protons, and two electrons. The enzyme is composed of an 88.7-kDa molybdoprotein (L), a 30.2-kDa flavoprotein (M), and a 17.8-kDa iron–sulfur protein (S) and is organized as a dimer of LMS heterotrimers. The active site of CODH consists of a binuclear heterometal [CuSMo(=O)OH] cluster that is prone to cyanolysis. The cluster is coordinated through interactions of the molybdenum with the dithiolate pyran ring of molybdopterin cytosine dinucleotide and of the copper with Sγ of Cys388; the two metals are bridged by a sulfido-ligand. A model for the catalytic cycle involves a thiocarbonate-like intermediate state and includes the transfer of two electrons from Mo through two types of [2Fe–2S]-clusters to the flavin–adenine dinucleotide cofactor.

3D Structure


  • molybdenum/tungsten;
  • enzyme;
  • carbon monoxide (CO) dehydrogenase (CODH);
  • E.C.