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Updated: Aug 14, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate
Jongyun Heo1, Lars Skjeldal, Christopher R Staples
1Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, 53706-1544, USA.
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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