Construction of a bisaquo heme enzyme and binding by exogenous ligands.
The crystal structure of the His-175-->Gly (H175G) mutant of cytochrome-c peroxidase (EC 1.11.1.5), missing its only heme ligand, reveals that the histidine is replaced by solvent to give a bisaquo heme protein. This protein retains some residual activity, which can be stimulated or inhibited by add...
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| 發表在: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , , , |
| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
National Academy of Sciences
1994
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| 主題: | |
| 在線閱讀: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC45537/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7809133/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.91.26.12847 |
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