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Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent hemes
In the absence of its substrate, the autoreduction of the high-valent bis-Fe(IV) state of the diheme enzyme MauG is coupled to oxidative damage of a methionine residue. Transient kinetic and solvent isotope effect studies reveal that this process occurs via two sequential long-range electron transfe...
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| Vydáno v: | Biochem J |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2016
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4903885/ https://ncbi.nlm.nih.gov/pubmed/27076451 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BCJ20160047 |
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