ArticleJournal of the American Chemical Society2010
Active site threonine facilitates proton transfer during dioxygen activation at the diiron center of toluene/o-xylene monooxygenase hydroxylase.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- Heme oxygenase-like dimetal oxidases and oxygenases.Biochemical Society transactions · 2026Review
- In Silico Investigation of Potential Applications of Gamma Carbonic Anhydrases as Catalysts of COInternational journal of molecular sciences · 2021Article
- Proton-Electron Transfer to the Active Site Is Essential for the Reaction Mechanism of Soluble ΔJournal of the American Chemical Society · 2020Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Article
- Coupling Oxygen Consumption with Hydrocarbon Oxidation in Bacterial Multicomponent Monooxygenases.Accounts of chemical research · 2015Article
- Single Turnover Reveals Oxygenated Intermediates in Toluene/o-Xylene Monooxygenase in the Presence of the Native Redox Partners.Journal of the American Chemical Society · 2015Article
- Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.Nature communications · 2014Article
- A flexible glutamine regulates the catalytic activity of toluene o-xylene monooxygenase.Biochemistry · 2014Article
- Article
- Article
- Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites.Journal of inorganic biochemistry · 2011Review
- Tracking a defined route for O₂ migration in a dioxygen-activating diiron enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylase.Biochemistry · 2011Article
- Characterization of a high-spin non-heme Fe(III)-OOH intermediate and its quantitative conversion to an Fe(IV)═O complex.Journal of the American Chemical Society · 2011Article
- Insights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylases.Journal of the American Chemical Society · 2011Article
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8 authors at 3 institutions in 1 country.
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Abstract
Toluene/o-xylene monooxygenase hydroxylase (ToMOH), a diiron-containing enzyme, can activate dioxygen to oxidize aromatic substrates. To elucidate the role of a strictly conserved T201 residue during dioxygen activation of the enzyme, T201S, T201G, T201C, and T201V variants of ToMOH were prepared by site-directed mutagenesis. X-ray crystal structures of all the variants were obtained. Steady-state activity, regiospecificity, and single-turnover yields were also determined for the T201 mutants. Dioxygen activation by the reduced T201 variants was explored by stopped-flow UV-vis and Mössbauer spectroscopy. These studies demonstrate that the dioxygen activation mechanism is preserved in all T201 variants; however, both the formation and decay kinetics of a peroxodiiron(III) intermediate, T201(peroxo), were greatly altered, revealing that T201 is critically involved in dioxygen activation. A comparison of the kinetics of O(2) activation in the T201S, T201C, and T201G variants under various reaction conditions revealed that T201 plays a major role in proton transfer, which is required to generate the peroxodiiron(III) intermediate. A mechanism is postulated for dioxygen activation, and possible structures of oxygenated intermediates are discussed.
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