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Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium Between Hemes with Only One Heme Exclusively Binding Exogenous Ligands

MauG is a diheme enzyme that oxidizes two protein-bound tryptophan residues to generate a catalytic tryptophan tryptophylquinone cofactor within methylamine dehydrogenase. Upon the two-electron oxidation of bis-ferric MauG, the two c-type hemes exist as a spin-uncoupled bis-Fe(IV) species with only...

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Detalhes bibliográficos
Main Authors: Fu, Rong, Liu, Fange, Davidson, Victor L., Liu, Aimin
Formato: Artigo
Idioma:Inglês
Publicado em: 2009
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2801551/
https://ncbi.nlm.nih.gov/pubmed/19911786
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi9017544
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