ArticleAngewandte Chemie (International ed. in English)2015
Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed.
- Indole N-Linked Hydroperoxyl Adduct of Protein-Derived Cofactor Modulating Catalase-Peroxidase Functions.Angewandte Chemie (International ed. in English) · 2024Article
- Capturing aBiochemistry · 2023Article
- 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
- Radical Trapping Study of the Relaxation ofReactive oxygen species (Apex, N.C.) · 2018Article
- Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 fromThe 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
- Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Journal of inorganic biochemistry · 2017Article
- Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.The Biochemical journal · 2016Article
- Rational Design of Dual Active Sites in a Single Protein Scaffold: A Case Study of Heme Protein in Myoglobin.ChemistryOpen · 2016Article
- Oxidation triggers extensive conjugation and unusual stabilization of two di-heme dication diradical intermediates: role of bridging group for electronic communication.Chemical science · 2016Article
- Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer.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
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3 authors.
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Abstract
The biosynthesis of tryptophan tryptophylquinone, a protein-derived cofactor, involves a long-range reaction mediated by a bis-Fe(IV) intermediate of a diheme enzyme, MauG. Recently, a unique charge-resonance (CR) phenomenon was discovered in this intermediate, and a biological, long-distance CR model was proposed. This model suggests that the chemical nature of the bis-Fe(IV) species is not as simple as it appears; rather, it is composed of a collection of resonance structures in a dynamic equilibrium. Here, we experimentally evaluated the proposed CR model by introducing small molecules to, and measuring the temperature dependence of, bis-Fe(IV) MauG. Spectroscopic evidence was presented to demonstrate that the selected compounds increase the decay rate of the bis-Fe(IV) species by disrupting the equilibrium of the resonance structures that constitutes the proposed CR model. The results support this new CR model and bring a fresh concept to the classical CR theory.
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