Title
MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis
Abbreviated Journal Title
Arch. Biochem. Biophys.
Keywords
Electron transfer; Posttranslational modification; Protein radical; Peroxidase; Oxygenase; High-valence iron; ELECTRON-TRANSFER REACTIONS; C-TYPE CYTOCHROMES; METHYLAMINE; DEHYDROGENASE; PARACOCCUS-DENITRIFICANS; DIFFERENT FORMS; SPIN HEME; PROTEIN; MECHANISM; COFACTOR; COMPLEX; Biochemistry & Molecular Biology; Biophysics
Abstract
MauG contains two c-type hemes with atypical physical and catalytic properties. While most c-type cytochromes function simply as electron transfer mediators, MauG catalyzes the completion of tryptophan tryptophylquinone (TFQ)(1) biosynthesis within a precursor protein of methylamine dehydrogenase. This posttranslational modification is a six-electron oxidation that requires crosslinking of two Trp residues, oxygenation of a Trp residue and oxidation of the resulting quinol to ITQ. These reactions proceed via a bis-Fe-IV state in which one heme is present as Fe-IV=O and the other is Fe-IV with axial heme ligands provided by His and Tyr side chains. Catalysis does not involve direct contact between the protein substrate and either heme of MauG. Instead it is accomplished by remote catalysis using a hole hopping mechanism of electron transfer in which Trp residues of MauG are reversibly oxidized. In this process, long range electron transfer is coupled to the radical mediated chemical reactions that are required for TTQ biosynthesis. (C) 2013 Elsevier Inc. All rights reserved.
Journal Title
Archives of Biochemistry and Biophysics
Volume
544
Publication Date
1-1-2014
Document Type
Review
Language
English
First Page
112
Last Page
118
WOS Identifier
ISSN
0003-9861
Recommended Citation
"MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis" (2014). Faculty Bibliography 2010s. 6084.
https://stars.library.ucf.edu/facultybib2010/6084
Comments
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