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How Does Tyrosinase Work? Recent Insights from Model Chemistry and Structural Biology
Author(s) -
Decker Heinz,
Dillinger Renée,
Tuczek Felix
Publication year - 2000
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/(sici)1521-3773(20000502)39:9<1591::aid-anie1591>3.0.co;2-h
Subject(s) - tyrosinase , copper , chemistry , substrate (aquarium) , structural biology , stereochemistry , biochemistry , enzyme , biology , ecology , organic chemistry
What is the hydroxylating species and how is the phenolic substrate bound to tyrosinase? Answers to these questions are promised by comparison of results from studies of model complexes with crystal structures of type 3 copper proteins. The present understanding of bonding (see picture) and conversion of substrates at binuclear, oxygen‐activating copper active sites is described.