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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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Detalhes bibliográficos
Main Authors: Geng, Jiafeng, Dornevil, Kednerlin, Davidson, Victor L., Liu, Aimin
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2013
Assuntos:
Acesso em linha: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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