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Properties of a Thermostable Nitrate Reductase from the Hyperthermophilic Archaeon Pyrobaculum aerophilum
The nitrate reductase of the hyperthermophilic archaeon Pyrobaculum aerophilum was purified 137-fold from the cytoplasmic membrane. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis, the enzyme complex consists of three subunits with apparent molecular weights of 130,000, 5...
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| Main Authors: | , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Society for Microbiology
2001
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC95438/ https://ncbi.nlm.nih.gov/pubmed/11544209 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.183.19.5491-5495.2001 |
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