Oxygen intermediates exhibit unique spectroscopic features which reflect novel geometric and electronic structures that are key to reactivity. This seminar will describe: 1) The bonding origin of the unique spectroscopic features of the coupled binuclear copper enzymes and how this overcomes the spin forbiddeness of O2 bonding and leads to activating monooxygenase activity; 2) How the difference in exchange coupling in the non-coupled binuclear Cu enzymes controls the reaction mechanism; and 3) How the trinuclear Cu cluster present in the multicopper oxidases leads to a major structure/function difference in enabling the reductive cleavage of the O-O bond with little overpotential and generating a fully oxidized intermediate, different from the resting enzyme studied by crystallography, that is key in enabling fast PCET in the reductive half of the catalytic cycle.

Award Address (Alfred Bader Award in Bioinorganic or Bioorganic Chemistry sponsored by the Alfred R. Bader Fund). Dioxygen binding, activation, and reduction to H2O by Cu enzymes

251st National Meeting (2016)

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