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

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...

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Veröffentlicht in:	Angewandte Chemie (International ed.) 2010-08, Vol.49 (36), p.6438-6442
Hauptverfasser:	Rolff, Malte, Schottenheim, Julia, Peters, Gerhard, Tuczek, Felix
Format:	Artikel
Sprache:	eng
Schlagworte:	Benzoquinones - chemistry Biocatalysis bioinorganic chemistry Coordination Complexes - chemistry Copper - chemistry enzymes homogeneous catalysis Kinetics Models, Biological Monophenol Monooxygenase - chemistry Monophenol Monooxygenase - metabolism Phenols - chemistry type 3 copper proteins tyrosinases
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Zusammenfassung:	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.
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201000973