The First Catalytic Tyrosinase Model System Based on a Mononuclear Copper(I) Complex: Kinetics and Mechanism

Authors


  • The authors acknowledge synthetic and/or spectroscopic support from Ursula Cornelissen, Stephanie Pehlke, Marianne Karbstein, and Franziska Wendt.

Abstract

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Ready… steady… go! The copper(I) complex 1 not only catalyzes the oxygenation of di-tert-butylphenol (DTBP-H) to di-tert-butylquinone (DTBQ) in a tyrosinase-like fashion, but also allows the reactive cycle to be studied in a stepwise and controlled manner. This feature opens new insights into the individual stages of the tyrosinase reaction, phenol hydroxylation, and release of the product as quinone. The implications for the enzymatic reaction are discussed.

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