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Hydrophobic Effect Drives Oxygen Uptake in Myoglobin via Histidine E7
Since the elucidation of the myoglobin (Mb) structure, a histidine residue on the E helix (His-E7) has been proposed to act as a gate with an open or closed conformation controlling access to the active site. Although it is believed that at low pH, the His-E7 gate is in its open conformation, the fu...
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| Главные авторы: | , , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Biochemistry and Molecular Biology
2013
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3585112/ https://ncbi.nlm.nih.gov/pubmed/23297402 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.426056 |
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