Abstract
The multicopper oxidases are an intriguing, widespread family of enzymes that catalyze the reduction of O2 to water by a variety of single-electron and multiple-electron reducing agents. The structure and properties of the copper binding sites responsible for the latter chemical transformations have been studied for over 40years and a detailed picture is emerging. This review focuses particularly on the kinetics of internal electron transfer between the type1 (blue) copper site and the trinuclear center, as well as on the nature of the intermediates formed in the oxygen reduction process.
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