Peroxomanganese intermediates are proposed in many catalytic redox reactions governed by manganese enzymes, such as manganese superoxide dismutase, manganese homoprotocatechuate 2,3-dioxygenase, and ribonucleotide reductases. The geometric and electronic factors governing O-O bond activation of peroxomanganese(III) species are poorly understood. We are investigating this area using a bio-inspired peroxomanganese(III) complex supported by the neutral cross-clamped cyclam ligand Me<sub>2</sub>EBC. The geometric and electronic structure of this peroxomanganese(III) adduct has been spectroscopically and computationally investigated and the subsequent activation of the peroxo unit explored through mechanistic and reactivity studies. In particular, chemically controlled cleavage of the O-O bond of the peroxomanganese(III) adduct is examined to further the understanding of the factors controlling O-O versus Mn-O bond cleavage for peroxomanganese(III) adducts.

Formation, characterization, and O-O bond activation of a bio-inspired peroxomanganese(III) complex

249th National Meeting (2015)

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