ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2016
Structure/function correlations over binuclear non-heme iron active sites.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2016. 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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16 citing papers in PubMed.
- OAngewandte Chemie (International ed. in English) · 2026Article
- Eating the brain - A multidisciplinary study provides new insights into the mechanisms underlying the cytopathogenicity of Naegleria fowleri.PLoS pathogens · 2025Article
- Spectroscopic definition of ferrous active sites in non-heme iron enzymes.Methods in enzymology · 2024Article
- Generation of a μ-1,2-hydroperoxo FeNature communications · 2022Article
- Nuclear Resonance Vibrational Spectroscopic Definition of the Fe(IV)Journal of the American Chemical Society · 2021Article
- Ligand-Constraint-Induced Peroxide Activation for Electrophilic Reactivity.Angewandte Chemie (International ed. in English) · 2021Article
- A Peroxodiiron(III/III) Intermediate Mediating BothJournal of the American Chemical Society · 2020Article
- De Novo Design of Four-Helix Bundle Metalloproteins: One Scaffold, Diverse Reactivities.Accounts of chemical research · 2019Article
- Spectroscopy and DFT Calculations of Flavo-Diiron Nitric Oxide Reductase Identify Bridging Structures of NO-Coordinated Diiron Intermediates.ACS catalysis · 2018Article
- Diiron monooxygenases in natural product biosynthesis.Natural product reports · 2018Review
- Structure, function and evolution of the hemerythrin-like domain superfamily.Protein science : a publication of the Protein Society · 2018Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Spectroscopy and DFT Calculations of a Flavo-diiron Enzyme Implicate New Diiron Site Structures.Journal of the American Chemical Society · 2017Article
- Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF.Journal of the American Chemical Society · 2017Article
- Article
- 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
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Abstract
Binuclear non-heme iron enzymes activate O2 to perform diverse chemistries. Three different structural mechanisms of O2 binding to a coupled binuclear iron site have been identified utilizing variable-temperature, variable-field magnetic circular dichroism spectroscopy (VTVH MCD). For the μ-OH-bridged Fe(II)2 site in hemerythrin, O2 binds terminally to a five-coordinate Fe(II) center as hydroperoxide with the proton deriving from the μ-OH bridge and the second electron transferring through the resulting μ-oxo superexchange pathway from the second coordinatively saturated Fe(II) center in a proton-coupled electron transfer process. For carboxylate-only-bridged Fe(II)2 sites, O2 binding as a bridged peroxide requires both Fe(II) centers to be coordinatively unsaturated and has good frontier orbital overlap with the two orthogonal O2 π* orbitals to form peroxo-bridged Fe(III)2 intermediates. Alternatively, carboxylate-only-bridged Fe(II)2 sites with only a single open coordination position on an Fe(II) enable the one-electron formation of Fe(III)-O2 (-) or Fe(III)-NO(-) species. Finally, for the peroxo-bridged Fe(III)2 intermediates, further activation is necessary for their reactivities in one-electron reduction and electrophilic aromatic substitution, and a strategy consistent with existing spectral data is discussed.
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