Work

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

Year: 2012

Type: article

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.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2012.10.044

Authors: Nafez Abu Tarboush, Sooim Shin, Jiafeng Geng, Aimin Liu, Victor L. Davidson

Institutions: University of Jordan, University of Central Florida, Georgia State University

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze