Tyrosinase-like reactivity in a Cu^III₂(μ-O) ₂ species

A study was conducted to demonstrate a bis(μ-oxo)dicopper(III) species that binds and ortho-hydroxylates phenolates for reactivity of tyrosinase. The study characterized a metastable species from the low-temperature reaction of sodium p-chloro-phenolate (p-Cl-C₆H₄ONa) with a bis(μ-oxo)dicopper(III) species. The study found that the addition of 10 equivalents of the sodium salt of p-chlorophenol at -90°C can cause bleaching of the spectral features. High performance liquid chromatography (HPLC) analysis showed that 4-chlorocatechol was formed in 76% yield. The study used UV/UVis monitoring for reaction in acetone to determine the initial features to the bis(μ-oxo) species and found that these features disappear after phenolate addition. The study observed that the activation parameters for the monophenolase reaction catalyzed by tyrosinase.