Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate
| Autor: | Lars Skjeldal, Christopher R. Staples, Jongyun Heo, Paul W. Ludden |
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| Rok vydání: | 2002 |
| Předmět: |
Magnetic Resonance Spectroscopy
Formates Stereochemistry Iron Side reaction Rhodospirillum rubrum Photochemistry Biochemistry Catalysis Inorganic Chemistry chemistry.chemical_compound Multienzyme Complexes Nickel Formate Cyanides biology Sulfates Chemistry Active site biology.organism_classification Aldehyde Oxidoreductases biology.protein Protons Oxidation-Reduction Carbon monoxide dehydrogenase |
| Zdroj: | JBIC Journal of Biological Inorganic Chemistry. 7:810-814 |
| ISSN: | 1432-1327 0949-8257 |
| DOI: | 10.1007/s00775-002-0365-z |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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