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Thermal stability of Clostridium pasteurianum rubredoxin: deconvoluting the contributions of the metal site and the protein.
To provide a framework for understanding the hyperthermostability of some rubredoxins, a comprehensive analysis of the thermally induced denaturation of rubredoxin (Rd) from the mesophile, Clostridium pasteurianum was undertaken. Rds with three different metals in its M(SCys)4 site (M = Fe3+/2+, Zn2...
Tallennettuna:
| Päätekijät: | , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Cold Spring Harbor Laboratory Press
2000
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2144531/ https://ncbi.nlm.nih.gov/pubmed/11206063 |
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