Oxygen Binding, Activation, and Reduction to Water by Copper Proteins.
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.
Solomon
Edward I.
EI
Department of Chemistry Stanford University Stanford, CA 94305 (USA).
Chen
Peng
P
Metz
Markus
M
Lee
Sang-Kyu
SK
Palmer
Amy E.
AE