Dual oxidase/oxygenase reactivity and resonance Raman spectra of {Cu3O2} moiety with perfluoro-t-butoxide ligands

Abstract

A Cu(I) fully fluorinated O-donor monodentate alkoxide complex, K[Cu(OC₄F₉)₂], was previously shown to form a trinuclear copper–dioxygen species with a {Cu₃(μ₃-O)₂} core, T_OC4F9, upon reactivity with O₂ at low temperature. Herein is reported a significantly expanded kinetic and mechanistic study of T_OC4F9 formation using stopped-flow spectroscopy. The T_OC4F9 complex performs catalytic oxidase conversion of hydroquinone (H₂Q) to benzoquinone (Q). T_OC4F9 also demonstrated hydroxylation of 2,4-di-tert-butylphenolate (DBP) to catecholate, making T_OC4F9 the first trinuclear species to perform tyrosinase (both monooxygenase and oxidase) chemistry. Resonance Raman spectra were also obtained for T_OC4F9, to our knowledge, the first such spectra for any T species. The mechanism and substrate reactivity of T_OC4F9 are compared to those of its bidentate counterpart, T_pin^F, formed from K[Cu(pin^F)(PR₃)]. The monodentate derivative has both faster initial formation and more diverse substrate reactivity.