ArticleBiochemistry2012
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.Nature communications · 2019Article
- Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Biochemistry · 2018Review
- Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.The Biochemical journal · 2017Article
- Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.FEBS letters · 2017Article
- Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Journal of inorganic biochemistry · 2017Article
- A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Biochemistry · 2016Article
- Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.The Biochemical journal · 2016Article
- Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.Biochimica et biophysica acta · 2015Article
- Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.Angewandte Chemie (International ed. in English) · 2015Article
- Bis-Fe(IV): nature's sniper for long-range oxidation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.Biochemistry · 2014Article
- MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Archives of biochemistry and biophysics · 2014Review
- Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways.Biochemistry · 2013Article
- Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.Biochemistry · 2013Article
- A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis.FEBS letters · 2013Article
- Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.Dalton transactions (Cambridge, England : 2003) · 2013Review
- Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.Annual review of biochemistry · 2013Review
- Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.FEBS letters · 2012Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
The diheme enzyme MauG catalyzes a six-electron oxidation required for posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. Crystallographic studies had shown that Pro107, which resides in the distal pocket of the high-spin heme of MauG, changes conformation upon binding of CO or NO to the heme iron. In this study, Pro107 was converted to Cys, Val, and Ser by site-directed mutagenesis. The structures of each of these MauG mutant proteins in complex with preMADH were determined, as were their physical and catalytic properties. P107C MauG was inactive, and the crystal structure revealed that Cys107 had been oxidatively modified to a sulfinic acid. Mass spectrometry revealed that this modification was present prior to crystallization. P107V MauG exhibited spectroscopic and catalytic properties that were similar to those of wild-type MauG, but P107V MauG was more susceptible to oxidative damage. The P107S mutation caused a structural change that resulted in the five-coordinate high-spin heme being converted to a six-coordinate heme with a distal axial ligand provided by Glu113. EPR and resonance Raman spectroscopy revealed this heme remained high-spin but with greatly increased rhombicity as compared to that of the axial signal of wild-type MauG. P107S MauG was resistant to reduction by dithionite and reaction with H(2)O(2) and unable to catalyze TTQ biosynthesis. These results show that the presence of Pro107 is critical in maintaining the proper structure of the distal heme pocket of the high-spin heme of MauG, allowing exogenous ligands to bind and directing the reactivity of the heme-activated oxygen during catalysis, thus minimizing the oxidation of other residues of MauG.
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