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Back Cover: Catalytic Phenol Hydroxylation with Dioxygen: Extension of the Tyrosinase Mechanism beyond the Protein Matrix (Angew. Chem. Int. Ed. 20/2013)
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.201303052
Subject(s) - tyrosinase , hydroxylation , chemistry , catalysis , substrate (aquarium) , mechanism (biology) , combinatorial chemistry , biocatalysis , cover (algebra) , catechol oxidase , int , enzyme , stereochemistry , reaction mechanism , organic chemistry , polyphenol oxidase , computer science , biology , mechanical engineering , ecology , philosophy , epistemology , engineering , peroxidase , operating system
Translating the catalytic mechanism of an enzyme to a synthetic complex is a challenging endeavor. In their Communication on page 5398 ff., S. Herres‐Pawlis, T. D. P. Stack, and co‐workers present a complex capable of the efficient catalytic oxidation of phenols to quinones by using dioxygen. The mechanism of the synthetic system is similar to that of tyrosinase, yet the substrate scope extends beyond that of the enzyme. Thus this work fulfills a goal of bioinspired chemistry.