Oxidation of CO to CO2 by CO dehydrogenases: Enzymology, mechanism, and posttranslational maturation

FUEL 183

Ortwin O. Meyer, ortwin.meyer@uni-bayreuth.de, Astrid M. Pelzmann, and Vitali A. Svetlitchnyi. Department of Microbiology, University of Bayreuth, Universitätsstrasse 30, D-95447 Bayreuth, Germany
Carbon monoxide dehydrogenases (CODHs)are structurally resolved metalloproteins functioning in aerobic and anaerobic chemolithoautotrophic bacteria and archaea. They catalyze the oxidation of the highly toxic poison gas CO to CO2 and play an important role in climate related cycles of atmospheric gases. Two main classes of CODHs can be distinguished. The heterohexameric enzymes from aerobic bacteria and the homodimeric enzymes from anaerobic bacteria or archaea. The former contain a unique [CuSMoO2] cluster in their active site, whereas the latter employ a unique [Ni-4Fe-5S] cluster. Studies employing compounds structurally related to CO have generated information on the interaction of CO at these metal active sites and how the reaction product CO2 is being formed. These clusters are subject to posttranslational maturation which is another topic to be discussed.