A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state
Keywords: TTQ, tryptophan tryptophylquinone; MADH, methylamine dehydrogenase; preMADH, the biosynthetic precursor protein of MADH with incompletely synthesized TTQ; bis-Fe(IV) MauG, redox state of MauG with one heme as Fe(IV)O and the other as Fe(IV); ET, electron