Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity
Abbreviated Journal Title
Cytochrome c; High-valence Fe; Redox enzyme; Tryptophan; tryptophylquinone; TRYPTOPHAN TRYPTOPHYLQUINONE BIOSYNTHESIS; CYTOCHROME-C PEROXIDASE; METHYLAMINE DEHYDROGENASE; DIFFERENT FORMS; COMPOUND-I; BIOGENESIS; LIGATION; COFACTOR; SPECTRA; COMPLEX; Biochemistry & Molecular Biology; Biophysics; Cell Biology
MauG catalyzes posttranslational modifications of methylamine dehydrogenase to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. MauG possesses a five-coordinate high-spin and a six-coordinate low-spin ferric heme, the latter with His-Tyr ligation. Replacement of this tyrosine with lysine generates a MauG variant with only high-spin ferric heme and altered spectroscopic and redox properties. Y294K MauG cannot stabilize the bis-Fe(IV) redox state required for TTQ biosynthesis but instead forms a compound I-like species on reaction with peroxide. The results clarify the role of Tyr ligation of the five-coordinate heme in determining the physical and redox properties and reactivity of MauG. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
"Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity" (2012). Faculty Bibliography 2010s. 2191.