ArticleInorganic chemistry2012
Protonation of a peroxodiiron(III) complex and conversion to a diiron(III/IV) intermediate: implications for proton-assisted O-O bond cleavage in nonheme diiron enzymes.
Article in Inorganic chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Article
- Nature of the Reactive Biferric Peroxy Intermediate P' in the Arylamine Oxygenases and Related Binuclear Fe Enzymes.Journal of the American Chemical Society · 2025Article
- Preparations ofMolecules (Basel, Switzerland) · 2023Article
- Stoichiometric Alkane and Aldehyde Hydroxylation Reactions Mediated by In Situ Generated Iron(III)-Iodosylbenzene Adduct.Molecules (Basel, Switzerland) · 2023Article
- Explorations of the nonheme high-valent iron-oxo landscape: crystal structure of a synthetic complex with an [FeIV2(μ-O)Faraday discussions · 2022Article
- Generation of a μ-1,2-hydroperoxo FeNature communications · 2022Article
- A Reactive, Photogenerated High-Spin (Journal of the American Chemical Society · 2021Article
- BesC Initiates C-C Cleavage through a Substrate-Triggered and Reactive Diferric-Peroxo Intermediate.Journal of the American Chemical Society · 2021Article
- Mechanistic Insights into Iron-Catalyzed C-H Bond Activation and C-C Coupling.Organometallics · 2021Article
- A nonheme peroxo-diiron(III) complex exhibiting both nucleophilic and electrophilic oxidation of organic substrates.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Iron Oxidation inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- Iron Oxidation in Escherichia coli Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with HAngewandte Chemie (International ed. in English) · 2021Article
- ScJournal of the American Chemical Society · 2020Article
- Activation of Dioxygen by a Mononuclear Nonheme Iron Complex: Sequential Peroxo, Oxo, and Hydroxo Intermediates.Journal of the American Chemical Society · 2019Article
- Diiron monooxygenases in natural product biosynthesis.Natural product reports · 2018Review
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Hydrogen-Atom Transfer Oxidation with HIsrael journal of chemistry · 2017Article
- Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Journal of the American Chemical Society · 2017Article
- X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Conversion of Aldehyde to Alkane by a Peroxoiron(III) Complex: A Functional Model for the Cyanobacterial Aldehyde-Deformylating Oxygenase.Journal of the American Chemical Society · 2015Article
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Abstract
Oxygenation of a diiron(II) complex, [Fe(II)(2)(μ-OH)(2)(BnBQA)(2)(NCMe)(2)](2+) [2, where BnBQA is N-benzyl-N,N-bis(2-quinolinylmethyl)amine], results in the formation of a metastable peroxodiferric intermediate, 3. The treatment of 3 with strong acid affords its conjugate acid, 4, in which the (μ-oxo)(μ-1,2-peroxo)diiron(III) core of 3 is protonated at the oxo bridge. The core structures of 3 and 4 are characterized in detail by UV-vis, Mössbauer, resonance Raman, and X-ray absorption spectroscopies. Complex 4 is shorter-lived than 3 and decays to generate in ~20% yield of a diiron(III/IV) species 5, which can be identified by electron paramagnetic resonance and Mössbauer spectroscopies. This reaction sequence demonstrates for the first time that protonation of the oxo bridge of a (μ-oxo)(μ-1,2-peroxo)diiron(III) complex leads to cleavage of the peroxo O-O bond and formation of a high-valent diiron complex, thereby mimicking the steps involved in the formation of intermediate X in the activation cycle of ribonucleotide reductase.
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