Evidence for H-bonding interactions to the μ-η2:η2-peroxide of oxy-tyrosinase that activate its coupled binuclear copper site.
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DOI: 10.1039/d2cc00750a
Abstract: 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… read more here.
Keywords: oxy tyrosinase; coupled binuclear; peroxide oxy; bonding interactions ... See more keywords