Evidence for H-bonding interactions to the μ-η2:η2-peroxide of oxy-tyrosinase that activate its coupled binuclear copper site

The factors that control the diverse reactivity of the mu-eta(2):eta(2)-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 mu-eta(2):eta(2)-peroxide of oxy-tyrosinase, and define their effects on the Cu(ii)(2)O-2 electronic structure and O-2 activation.

Automated summary

This study reveals the H-bonding interactions between active-site waters and the mu-eta(2):eta(2)-peroxide of oxy-tyrosinase, and defines their effects on the Cu(ii)(2)O-2 electronic structure and O-2 activation using spectroscopic and computational methods.