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...
Spremljeno u:
| Izdano u: | Proc Natl Acad Sci U S A |
|---|---|
| Glavni autori: | , , , , |
| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
National Academy of Sciences
1994
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| Teme: | |
| Online pristup: | 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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