Abstract
Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum reversibly catalyzes the oxidation of CO to CO(2) at the active site C-cluster. In this article, the reduction of CO(2) to formate is reported as a slow side reaction catalyzed by both Ni-containing CODH and Ni-deficient CODH. Recently, the structures of R. rubrum CODH and its active site NiFeS cluster (the C-cluster) have been solved. The data in this manuscript describe the formate-producing capability of CODH with or without Ni in the active site.
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Schedule a callMore From: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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