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Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG
The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone cofactor. The MauG-catalyzed reaction proceeds via a bis-Fe(IV) intermediate in which one heme is present as Fe(IV)=O and the other as Fe(IV) w...
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| Main Authors: | , , , |
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| Format: | Artigo |
| Language: | Inglês |
| Published: |
National Academy of Sciences
2013
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| Subjects: | |
| Online Access: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3683780/ https://ncbi.nlm.nih.gov/pubmed/23720312 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1301544110 |
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