ArticleBiochemistry2015
Rate-Determining Attack on Substrate Precedes Rieske Cluster Oxidation during Cis-Dihydroxylation by Benzoate Dioxygenase.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
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- Custom tuning of Rieske oxygenase reactivity.Nature communications · 2023Article
- Seeing theJournal of the American Chemical Society · 2023Article
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- Elucidating the Role of OACS environmental Au · 2022Article
- Substrate-Specific Coupling of OACS catalysis · 2022Article
- Quantitative 1H-NMR analysis reveals steric and electronic effects on the substrate specificity of benzoate dioxygenase in Ralstonia eutropha B9.Journal of industrial microbiology & biotechnology · 2022Article
- The Apparently Unreactive Substrate Facilitates the Electron Transfer for Dioxygen Activation in Rieske Dioxygenases.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Mechanisms of OBiochemistry · 2021Article
- Combinatorial pathway balancing provides biosynthetic access to 2-fluoro-Chem catalysis · 2021Article
- Structural and Biochemical Analysis Reveals a Distinct Catalytic Site of Salicylate 5-Monooxygenase NagGH from Rieske Dioxygenases.Applied and environmental microbiology · 2021Article
- Structural Studies of theBiochemistry · 2020Article
- Salicylate 5-Hydroxylase: Intermediates in Aromatic Hydroxylation by a Rieske Monooxygenase.Biochemistry · 2019Article
- Spectroscopic Characterisation of the Naphthalene Dioxygenase fromInternational journal of molecular sciences · 2019Article
- Review
- Nuclear Resonance Vibrational Spectroscopy Definition of OJournal of the American Chemical Society · 2018Article
- Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.Applied microbiology and biotechnology · 2018Review
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7 authors.
Funding
Abstract
Rieske dearomatizing dioxygenases utilize a Rieske iron-sulfur cluster and a mononuclear Fe(II) located 15 Å across a subunit boundary to catalyze O2-dependent formation of cis-dihydrodiol products from aromatic substrates. During catalysis, O2 binds to the Fe(II) while the substrate binds nearby. Single-turnover reactions have shown that one electron from each metal center is required for catalysis. This finding suggested that the reactive intermediate is Fe(III)-(H)peroxo or HO-Fe(V)═O formed by O-O bond scission. Surprisingly, several kinetic phases were observed during the single-turnover Rieske cluster oxidation. Here, the Rieske cluster oxidation and product formation steps of a single turnover of benzoate 1,2-dioxygenase are investigated using benzoate and three fluorinated analogues. It is shown that the rate constant for product formation correlates with the reciprocal relaxation time of only the fastest kinetic phase (RRT-1) for each substrate, suggesting that the slower phases are not mechanistically relevant. RRT-1 is strongly dependent on substrate type, suggesting a role for substrate in electron transfer from the Rieske cluster to the mononuclear iron site. This insight, together with the substrate and O2 concentration dependencies of RRT-1, indicates that a reactive species is formed after substrate and O2 binding but before electron transfer from the Rieske cluster. Computational studies show that RRT-1 is correlated with the electron density at the substrate carbon closest to the Fe(II), consistent with initial electrophilic attack by an Fe(III)-superoxo intermediate. The resulting Fe(III)-peroxo-aryl radical species would then readily accept an electron from the Rieske cluster to complete the cis-dihydroxylation reaction.
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