ArticleProceedings of the National Academy of Sciences of the United States of America2013
Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 67 citations in OpenAlex.
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- Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.Annual review of biophysics · 2022Review
- Copper binding by a unique family of metalloproteins is dependent on kynurenine formation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Spectroscopic evidence for direct flavin-flavin contact in a bifurcating electron transfer flavoprotein.The Journal of biological chemistry · 2020Article
- Carbon-fluorine bond cleavage mediated by metalloenzymes.Chemical Society reviews · 2020Review
- A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.Journal of the American Chemical Society · 2020Article
- MbnH is a diheme MauG-like protein associated with microbial copper homeostasis.The Journal of biological chemistry · 2019Article
- A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.Nature communications · 2019Article
- Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes.Archives of biochemistry and biophysics · 2018Review
- Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions.Biochemistry · 2018Review
- Mechanism for the depolymerization of cellulose under alkaline conditions.Journal of molecular modeling · 2018Article
- Distinct properties underlie flavin-based electron bifurcation in a novel electron transfer flavoprotein FixAB fromThe Journal of biological chemistry · 2018Article
- Radical Trapping Study of the Relaxation ofReactive oxygen species (Apex, N.C.) · 2018Article
- Mesna (2-mercaptoethane sodium sulfonate) functions as a regulator of myeloperoxidase.Free radical biology & medicine · 2017Article
- Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 fromThe Journal of biological chemistry · 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
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone cofactor. The MauG-catalyzed reaction proceeds via a bis-Fe(IV) intermediate in which one heme is present as Fe(IV)=O and the other as Fe(IV) with axial histidine and tyrosine ligation. Herein, a unique near-infrared absorption feature exhibited specifically in bis-Fe(IV) MauG is described, and evidence is presented that it results from a charge-resonance-transition phenomenon. As the two hemes are physically separated by 14.5 Å, a hole-hopping mechanism is proposed in which a tryptophan residue located between the hemes is reversibly oxidized and reduced to increase the effective electronic coupling element and enhance the rate of reversible electron transfer between the hemes in bis-Fe(IV) MauG. Analysis of the MauG structure reveals that electron transfer via this mechanism is rapid enough to enable a charge-resonance stabilization of the bis-Fe(IV) state without direct contact between the hemes. The finding of the charge-resonance-transition phenomenon explains why the bis-Fe(IV) intermediate is stabilized in MauG and does not permanently oxidize its own aromatic residues.
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