Activation of nit-1 nitrate reductase by W-formate dehydrogenase
| Autor: | Edward I. Solomon, Deloria B. Jacobs, Barbara K. Burgess, Joseph C. Deaton, Phyllis J. Wetherbee, Charles N. Durfor |
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| Rok vydání: | 1984 |
| Předmět: |
Biophysics
Formate dehydrogenase Nitrate reductase Biochemistry Cofactor chemistry.chemical_compound Tungstate Nitrate Reductases Sulfite oxidase Nitrogenase Molecular Biology Clostridium Neurospora crassa biology Active site Cell Biology equipment and supplies biology.organism_classification Aldehyde Oxidoreductases Formate Dehydrogenases Enzyme Activation chemistry Azotobacter vinelandii Azotobacter biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications. 121:1042-1047 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(84)90782-4 |
| Popis: | Formate dehydrogenase ( FDH ) from Clostridium thermoaceticum is a known tungsten enzyme. FDH was tested for the presence of nitrogenase-type cofactor and nitrate reductase-type cofactor by the Azotobacter vinelandii UW-45 and Neurospora crassa nit-1 reconstitution assays, respectively. Tungsten formate dehydrogenase (W- FDH ), containing only a small Mo impurity, activated the nit-1 nitrate reductase extracts when molybdate was also added, but not when tungstate was added. These results show W- FDH contains the cofactor common to all known Mo-enzymes except nitrogenase. The difference between the redox chemistries of W- FDH and W-substituted sulfite oxidase appears to relate to differences in tungsten ligation other than that donated by the cofactor or to variations in the protein environment surrounding the tungsten active site. |
| Databáze: | OpenAIRE |
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