Peroxomanganese(III) species are proposed as intermediates in many catalytic redox reactions governed by manganese enzymes, such as manganese superoxide dismutase, manganese homoprotocatechuate 2,3-dioxygenase, and manganese ribonucleotide reductase. While there are examples of synthetic models of these active sites and reactivity, the geometric and electronic factors that direct the reactivity of peroxomanganese(III) intermediates are poorly understood. We have generated and spectroscopically and computationally characterized a peroxomanganese(III) complex supported by the neutral cross-clamped cyclam ligand, Me2EBC. This ligand is known to support mononuclear, high-valent MnIV species with well-defined spectroscopic properties, which enables identification of MnIV intermediates formed from O—O bond cleavage of the MnIII-peroxo adduct. The decay products of the peroxomanganese(III) adduct indicate unique reactivity by avoiding dimanganese product formation and forming a mononuclear MnIII-hydroxo adduct or a mixture of mononuclear MnIV-oxo and MnIII-hydroxo species, depending on the reaction conditions.

Formation, characterization, and O-O bond activation of a peroxomanganese(III) complex supported by a cross-clamped cyclam ligand

251st National Meeting (2016)

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