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Radical Trapping Study of the Relaxation of bis-Fe(IV) MauG
The di-heme enzyme, MauG, utilizes a high-valent, charge-resonance stabilized bis-Fe(IV) state to perform protein radical-based catalytic chemistry. Though the bis-Fe(IV) species is able to oxidize remote tryptophan residues on its substrate protein, it does not rapidly oxidize its own residues in t...
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| Опубликовано в: : | React Oxyg Species (Apex) |
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| Главные авторы: | , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
2018
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5822730/ https://ncbi.nlm.nih.gov/pubmed/29479564 |
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