Copper-Oxygen Dynamics in the Tyrosinase Mechanism.

The dinuclear copper enzyme, tyrosinase, activates O to form a (μ-η :η -peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate l-tyrosine.