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Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate

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JBIC Journal of Biological Inorganic Chemistry Aims and scope Submit manuscript

Abstract.

Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum reversibly catalyzes the oxidation of CO to CO2 at the active site C-cluster. In this article, the reduction of CO2 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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Authors and Affiliations

  1. Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, Madison, WI 53706-1544, USA, , , , ,

    Jongyun Heo, Christopher R. Staples &  P. Ludden

  2. IKB, Box 5040, Agricultural University of Norway, NLH, 1432, Aas, Norway, , , , ,

    Lars Skjeldal

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  1. Jongyun Heo
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  2. Lars Skjeldal
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  3. Christopher R. Staples
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  4. P. Ludden
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Heo, J., Skjeldal, L., Staples, C.R. et al. Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate. J Biol Inorg Chem 7, 810–814 (2002). https://doi.org/10.1007/s00775-002-0365-z

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  • DOI: https://doi.org/10.1007/s00775-002-0365-z

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