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Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.
Dimethyl sulphoxide reductase was purified from the photosynthetic bacterium Rhodobacter capsulatus. The enzyme is composed of a single polypeptide of Mr 82,000 and contains a pterin-type molybdenum cofactor as the only detectable prosthetic group. The oxidized molybdenum cofactor of dimethyl sulpho...
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| Autors principals: | , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
1991
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1149954/ https://ncbi.nlm.nih.gov/pubmed/2001248 |
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