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Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation
Synechocystis hemoglobin contains an unprecedented covalent bond between a nonaxial histidine side chain (H117) and the heme 2-vinyl. This bond has been previously shown to stabilize the ferric protein against denaturation, and also to affect the kinetics of cyanide association. However, it is uncle...
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| Главные авторы: | , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Cold Spring Harbor Laboratory Press
2007
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2203299/ https://ncbi.nlm.nih.gov/pubmed/17242429 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.062572607 |
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