Copper(III) Intermediates in Tyrosinase Model

  • Author: Angewandte Chemie International Edition
  • Published Date: 26 August 2016
  • Source / Publisher: Angewandte Chemie International Edition/Wiley-VCH
  • Copyright: Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
thumbnail image: Copper(III) Intermediates in Tyrosinase Model

Tyrosinase enzymes (Ty), found in nearly all aerobic life forms, oxidize substrates through a binuclear copper active site that activates dioxygen. The resulting side-on peroxide CuII species converts tyrosine to melanins for pigment formation in animals and plants.

Daniel P. Stack, Stanford University, CA, USA, and colleagues have shown that the simplest synthetic active-site analogue (pictured) can be formed by a self-assembly process. Substituted imidazoles, CuI, and O2 organize in solution at a temperature of –145 °C. The substrate reactivity is similar to that of Ty but apparently proceeds through a mechanism not postulated for the biological oxidation.  The researchers charaterized a high-valent bis-CuIII bis-oxide intermediate.

While the assembly and CuIII identification are surprising, the stability and facile reactivity reveal a detail of Ty chemistry: The tertiary protein structure may not be needed, e.g., to impose structural constraints or induce function, since the active-site core is innately reactive.


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Magazine of Chemistry Europe (16 European Chemical Societies)published by Wiley-VCH