Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.
Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.
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DOI：
10.1016/j.febslet.2012.10.044
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发表时间：
2012-12-14
期刊：
影响因子：
3.5
通讯作者：
Davidson VL
中科院分区：
文献类型：
--
作者：
Abu Tarboush N;Shin S;Geng J;Liu A;Davidson VL
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.
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