TitleDatePubMed ID
Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.2017 Jun28485817
Free-Energy Landscape and Proton Transfer Pathways in Oxidative Deamination by Methylamine Dehydrogenase.2017 Jan 1827860041
Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.2014 Mar 424517455
MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.2014 Feb 1524144526
Identification of genes essential for the biogenesis of quinohemoprotein amine dehydrogenase.2014 Feb 1124437536
Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis.2013 Nov 1524024544
Structures of MauG in complex with quinol and quinone MADH.2013 Jul23832199
A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis.2013 Jun 1923669364
Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.2012 Sep 422897160
Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper.2011 Dec22071089