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A multiplet analysis of Fe K-edge 1s → 3d pre-edge features of iron complexes. Reactivity of hydroperoxide bound to a mononuclear non-heme iron site. The electronic structure of non-heme iron(III)-hydroperoxo and iron(III)-peroxo model complexes studied by Mössbauer and electron paramagnetic resonance spectroscopies. J., Banse, F., Girerd, J.-J., Wieghardt, K. Deprotonation of low-spin mononuclear iron(III)-hydroperoxide complexes give transient blue species assigned to high-spin iron(III)-peroxide complexes. Crystal structure of a metal ion-bound oxoiron(IV) complex and implications for biological electron transfer.
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Spectroscopic characterization of a hydroperoxo-heme intermediate: conversion of a side-on peroxo to an end-on hydroperoxo complex. Detailed spectroscopic and theoretical studies on 3–: electronic structure of the side-on ferric-peroxide bond and its relevance to reactivity. Variable character of O-O and M-O bonding in side-on (η 2) 1:1 metal complexes of O2. Mononuclear nonheme ferric-peroxo complex in aldehyde deformylation. Crystallographic and spectroscopic characterization of a nonheme Fe(IV) = O complex. Geometric and electronic structure and reactivity of a mononuclear ‘side-on’ nickel(III)-peroxo complex. Synthesis, structural, and spectroscopic characterization and reactivities of mononuclear cobalt(III)-peroxo complexes. +: a side-on peroxido manganese(III) complex bearing a non-heme ligand. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Crystal structures of Fe 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics. Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Geometric and electronic structure/function correlations in non-heme iron enzymes. These reactivity results demonstrate that iron( iii)–hydroperoxo species are viable oxidants in both nucleophilic and electrophilic reactions by iron-containing enzymes.
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We have performed relative reactivity studies on these three iron species which reveal that the iron( iii)–hydroperoxo complex is the most reactive of the three in the deformylation of aldehydes and that it has a similar reactivity to the iron( iv)–oxo complex in C–H bond activation of alkylaromatics. All three of these iron species-the three most biologically relevant iron–oxygen intermediates-have been spectroscopically characterized we note that they have been obtained using a simple macrocyclic ligand.
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This iron( iii)–hydroperoxo complex then cleanly converts to the ferryl complex, 2+, via homolytic O–O bond cleavage of the iron( iii)–hydroperoxo species.
#Iron reactivity series#
We also report a series of chemical reactions in which this iron( iii)–peroxo complex is cleanly converted to the iron( iii)–hydroperoxo complex, 2+, via a short-lived intermediate on protonation. Here we report the high-resolution crystal structure of a mononuclear non-haem side-on iron( iii)–peroxo complex, +. It has been difficult to generate synthetic analogues of these three active iron–oxygen species in identical host complexes, which is necessary to elucidate changes to the structure of the iron centre during catalysis and the factors that control their chemical reactivities with substrates. Oxygen-containing mononuclear iron species-iron( iii)–peroxo, iron( iii)–hydroperoxo and iron( iv)–oxo-are key intermediates in the catalytic activation of dioxygen by iron-containing metalloenzymes 1, 2, 3, 4, 5, 6, 7.