Title

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

Authors

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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