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The First Catalytic Tyrosinase Model System Based on a Mononuclear Copper(I) Complex: Kinetics and Mechanism
Author(s) -
Rolff Malte,
Schottenheim Julia,
Peters Gerhard,
Tuczek Felix
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201000973
Subject(s) - tyrosinase , hydroxylation , chemistry , quinone , catalytic cycle , kinetics , catalysis , biomimetic synthesis , copper , reaction mechanism , reactive intermediate , combinatorial chemistry , model system , stereochemistry , enzyme , organic chemistry , computational chemistry , physics , quantum mechanics
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.