Binuclear copper enzymes that activate dioxygen to form Cu-O2 species are capable of remarkably selective oxidations such as hydroxylating alkanes (alkane monooxygenases) or phenols (tyrosinases). Synthetic Cu-O2 species with closely related coordination environments provide keen insights into these biological oxidants and their reaction mechanisms. Self-assembly of an identically ligated side-on-peroxide oxidant from the simplest synthetic components along with its subsequent ability to hydroxylate phenols highlights its innate oxidative reactivity along with the potential role of Ntau imidazole ligation in stabilizing Cu(III) species. Similar insights are available from histamine ligation of Cu(III) akin to the coordination observed in the binuclear monooxygenases.

Cu(III) as a biological oxidant?

253rd National Meeting (2017)

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