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Redox-inactive metal ions that function as Lewis acids play pivotal roles in modulating reactivities of oxygen-containing metal complexes in a variety of biological and biomimetic reactions, including dioxygen activation/formation and functionalization of organic substrates. Mononuclear nonheme iron(III)-peroxo species are invoked as active oxygen intermediates in the catalytic cycles of dioxygen activation by nonheme iron enzymes and their biomimetic compounds. Here, we report mononuclear nonheme iron(III)-peroxo complexes binding redox-inactive metal ions, [(TMC)Fe III (O 2 )] + -M 3+ (M 3+ = Sc 3+ and Y 3+ ; TMC = 1,4,8,11-tetramethyl-1,4,8,11-tetraazacyclotetradecane), which are characterized spectroscopically as a 'side-on' iron(III)-peroxo complex binding a redox-inactive metal ion, (TMC)Fe III -(μ,η 2 :η 2 -O 2 )-M 3+ ( 2 -M). While an iron(III)-peroxo complex, [(TMC)Fe III (O 2 )] + , does not react with electron donors (e.g., ferrocene), one-electron reduction of the iron(III)-peroxo complexes binding redox-inactive metal ions occurs readily upon addition of electron donors, resulting in the generation of an iron(IV)-oxo complex, [(TMC)Fe IV (O)] 2+ ( 4 ), via heterolytic O-O bond cleavage of the peroxide ligand. The rates of the conversion of 2 -M to 4 are found to depend on the Lewis acidity of the redox-inactive metal ions and the oxidation potential of the electron donors. We have also determined the fundamental electron-transfer properties of 2 -M, such as the reduction potential and the reorganization energy in electron-transfer reaction. Based on the results presented herein, we have proposed a mechanism for the reactions of 2 -M and electron donors; the reduction of 2 -M to the reduced species, (TMC)Fe II -(O 2 )-M 3+ ( 2 '-M), is the rate-determining step, followed by heterolytic O-O bond cleavage of the reduced species to form 4 . The present results provide a biomimetic example demonstrating that redox-inactive metal ions bound to an iron(III)-peroxo intermediate play a significant role in activating the peroxide O-O bond to form a high-valent iron(IV)-oxo species.

A mononuclear nonheme iron(iii)–peroxo complex binding redox-inactive metal ions