The factors that control the diverse reactivity of the μ-η2:η2-peroxo dicopper(II) oxy-intermediates in the coupled binuclear copper proteins remain elusive. Here, spectroscopic and computational methods reveal H-bonding interactions between active-site waters and the μ-η2:η2-peroxide of oxy-tyrosinase, and define their effects on the Cu(II)2O2 electronic structure and O2 activation.

Department of Chemistry Stanford University Stanford California 94305 USA

Department of Chemistry Whitman College Walla Walla WA 99362 USA

Faculty of Science Charles University Albertov 2038 6 128 00 Praha 2 Czech Republic

Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences Flemingovo náměstí 2 166 10 Praha 6 Czech Republic

Stanford Synchrotron Radiation Lightsource SLAC National Accelerator Laboratory Stanford University Menlo Park California 94025 USA

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