Encyclopedia of Metalloproteins

2013 Edition
| Editors: Robert H. Kretsinger, Vladimir N. Uversky, Eugene A. Permyakov

CO-Dehydrogenase/Acetyl-CoA Synthase

  • Stephen W. Ragsdale
  • Elizabeth Pierce
  • Gunes Bender
Reference work entry
DOI: https://doi.org/10.1007/978-1-4614-1533-6_80



Carbon monoxide dehydrogenase (CODH) is a Ni–Fe4S4-dependent enzyme that catalyzes the interconversion of CO and CO2. Acetyl-CoA synthase (ACS) is a Ni–Ni–Fe4S4 dependent enzyme that synthesizes the central metabolite, acetyl-CoA, from CO, a methyl group from CFeSP, and CoA. CODH and ACS form a tightly bound bifunctional enzyme in Moorella thermoacetica.


Carbon monoxide dehydrogenase (CODH) allows microbes to extract CO from the air at the low levels present in the environment and use it as a sole source of carbon and energy (Fig.  1). Besides being a toxic gas, CO is a remarkably potent source of reducing equivalents; thus, the CODHs can couple CO oxidation to the reduction of various cellular redox systems (ferredoxin, hydrogenase, pyruvate synthase, etc.). Two types of CODH have been described: one harbors a molybdopterin/copper active site and the other contains a nickel–iron–sulfur cluster...
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Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  • Stephen W. Ragsdale
    • 1
  • Elizabeth Pierce
    • 1
  • Gunes Bender
    • 1
  1. 1.Department of Biological ChemistryUniversity of Michigan Medical SchoolAnn ArborUSA