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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… Click to show full 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 oxy-tyrosinase, and define their effects on the Cu(II)2O2 electronic structure and O2 activation.
Keywords:
oxy tyrosinase;
coupled binuclear;
peroxide oxy;
bonding interactions;
binuclear copper
Journal Title: Chemical communications
Year Published: 2022
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Journal Title: Chemical communications
Year Published: 2022
Link to full text (if available)
Share on Social Media: Sign Up to like & get
recommendations!