ArticleBiochemistry2013
Oxidative damage in MauG: implications for the control of high-valent iron species and radical propagation pathways.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Investigating the Ground-State and Ionization Processes of Hydrogen Peroxide Dimers Using Sequentially Combined Theoretical Approaches.Journal of chemical theory and computation · 2025Article
- Capturing aBiochemistry · 2023Article
- Electronic State of the His/Tyr-Ligated Heme of BthA by Mössbauer and DFT Analysis.Inorganic chemistry · 2020Article
- Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea.Archives of biochemistry and biophysics · 2019Article
- 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
- Radical Trapping Study of the Relaxation ofReactive oxygen species (Apex, N.C.) · 2018Article
- Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron hole-hopping within the enzyme.The Journal of biological chemistry · 2017Article
- 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
- LC-MS/MS suggests that hole hopping in cytochrome c peroxidase protects its heme from oxidative modification by excess HChemical science · 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
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The di-heme enzyme MauG catalyzes the oxidative biosynthesis of a tryptophan tryptophylquinone cofactor on a precursor of the enzyme methylamine dehydrogenase (preMADH). Reaction of H2O2 with the diferric form of MauG, or reaction of O2 with diferrous MauG, forms the catalytic intermediate known as bis-Fe(IV), which acts as the key oxidant during turnover. The site of substrate oxidation is more than 40 Å from the high-spin heme iron where H2O2 initially reacts, and catalysis relies on radical hopping through an interfacial residue, Trp199 of MauG. In the absence of preMADH, the bis-Fe(IV) intermediate is remarkably stable, but repeated exposure to H2O2 results in suicide inactivation. Using mass spectrometry, we show that this process involves the oxidation of three Met residues (108, 114, and 116) near the high-spin heme through ancillary electron transfer pathways engaged in the absence of substrate. The mutation of a conserved Pro107 in the distal pocket of the high-spin heme results in a dramatic increase in the level of oxidation of these Met residues. These results illustrate structural mechanisms by which MauG controls reaction with its high-valent heme cofactor and limits uncontrolled oxidation of protein residues and loss of catalytic activity. The conservation of Met residues near the high-spin heme among MauG homologues from different organisms suggests that eventual deactivation of MauG may function in a biological context. That is, methionine oxidation may represent a protective mechanism that prevents the generation of reactive oxygen species by MauG in the absence of preMADH.
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