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Catalytic Phenol Hydroxylation with Dioxygen: Extension of the Tyrosinase Mechanism beyond the Protein Matrix
Author(s) -
Hoffmann Alexander,
Citek Cooper,
Binder Stephan,
Goos Arne,
Rübhausen Michael,
Troeppner Oliver,
IvanovićBurmazović Ivana,
Wasinger Erik C.,
Stack T. Daniel P.,
HerresPawlis Sonja
Publication year - 2013
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.201301249
Subject(s) - hydroxylation , catalysis , tyrosinase , phenols , chemistry , ligand (biochemistry) , phenol , reaction mechanism , catechol oxidase , peroxide , catalytic cycle , active site , combinatorial chemistry , photochemistry , enzyme , organic chemistry , peroxidase , biochemistry , receptor , polyphenol oxidase
A new catalyst (see structure) hydroxylates phenols with O 2 via a stable side‐on peroxide complex, which is similar to the active site of tyrosinase in terms of the ligand environment and its spectroscopic properties. The catalytic oxidation of phenols to quinones proceeds at room temperature in the presence of NEt 3 and even non‐native substrates can be oxidized catalytically. The reaction mechanism is analogous to that of the enzyme‐catalyzed reaction.