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MD simulations and QM/MM calculations show that single-site mutations of cytochrome P450(BM3) alter the active site’s complexity and the chemoselectivity of oxidation without changing the active species
It is a long-standing mechanistic consensus that the mutation of the proton-shuttle mediator Threonine (T) in Cytochrome P450 enzymes severs the water channel and thereby quenches the formation of the active species: the high-valent iron(iv)-oxo porphyrin π-cation radical species, compound I (Cpd I)...
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| Publicado en: | Chem Sci |
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| Main Authors: | , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
Royal Society of Chemistry
2017
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5851339/ https://ncbi.nlm.nih.gov/pubmed/29568477 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c7sc01932g |
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