Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity

    Authors

    N. Abu Tarboush; S. Shin; J. F. Geng; A. M. Liu;V. L. Davidson

    Comments

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    Abbreviated Journal Title

    FEBS Lett.

    Keywords

    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

    Abstract

    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.

    Journal Title

    Febs Letters

    Volume

    586

    Issue/Number

    24

    Publication Date

    1-1-2012

    Document Type

    Article

    Language

    English

    First Page

    4339

    Last Page

    4343

    WOS Identifier

    WOS:000312004400014

    ISSN

    0014-5793

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