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Generation of a μ-1,2-hydroperoxo FeIIIFeIII and a μ-1,2-peroxo FeIVFeIII Complex

Stephan Walleck, Thomas Zimmermann, Henning Hachmeister, Christian Pilger, Thomas Huser, Sagie Katz, Peter Hildebrandt, Anja Stammler, Hartmut Bögge, Eckhard Bill, Thorsten Glaser

2022Nature Communications31 citationsDOIOpen Access PDF

Abstract

Abstract μ -1,2-Peroxo-diferric intermediates ( P ) of non-heme diiron enzymes are proposed to convert upon protonation either to high-valent active species or to activated P′ intermediates via hydroperoxo-diferric intermediates. Protonation of synthetic μ -1,2-peroxo model complexes occurred at the μ -oxo and not at the μ -1,2-peroxo bridge. Here we report a stable μ -1,2-peroxo complex {Fe III ( μ -O)( μ -1,2-O 2 )Fe III } using a dinucleating ligand and study its reactivity. The reversible oxidation and protonation of the μ -1,2-peroxo-diferric complex provide μ -1,2-peroxo Fe IV Fe III and μ -1,2-hydroperoxo-diferric species, respectively. Neither the oxidation nor the protonation induces a strong electrophilic reactivity. Hence, the observed intramolecular C-H hydroxylation of preorganized methyl groups of the parent μ -1,2-peroxo-diferric complex should occur via conversion to a more electrophilic high-valent species. The thorough characterization of these species provides structure-spectroscopy correlations allowing insights into the formation and reactivities of hydroperoxo intermediates in diiron enzymes and their conversion to activated P′ or high-valent intermediates.

Topics & Concepts

ProtonationElectrophileReactivity (psychology)HydroxylationChemistryLigand (biochemistry)StereochemistryReactive intermediatePhotochemistryIntramolecular forceReaction intermediateMedicinal chemistryCatalysisEnzymeOrganic chemistryBiochemistryPathologyIonMedicineReceptorAlternative medicineMetal-Catalyzed Oxygenation MechanismsPorphyrin and Phthalocyanine ChemistryMetalloenzymes and iron-sulfur proteins