title: Oxygen Binding, Activation, and Reduction to Water by Copper Proteins.
abstract: Copper active sites play a major role in biological and abiological dioxygen activation. Oxygen intermediates have been studied in detail for the proteins and enzymes involved in reversible O(2) binding (hemocyanin), activation (tyrosinase), and four-electron reduction to water (multicopper oxidases). These oxygen intermediates exhibit unique spectroscopic features indicative of new geometric and electronic structures involved in oxygen activation. The spectroscopic and quantum-mechanical study of these intermediates has defined geometric- and electronic-structure/function correlations, and developed detailed reaction coordinates for the reversible binding of O(2), hydroxylation, and H-atom abstraction from different substrates, and the reductive cleavage of the O-O bond in the formation water.
authors.affiliation: Department of Chemistry Stanford University Stanford, CA 94305 (USA).
authors.forename: Edward I.
authors.initials: EI
authors.lastname: Solomon
authors.forename: Peng
authors.initials: P
authors.lastname: Chen
authors.forename: Markus
authors.initials: M
authors.lastname: Metz
authors.forename: Sang-Kyu
authors.initials: SK
authors.lastname: Lee
authors.forename: Amy E.
authors.initials: AE
authors.lastname: Palmer