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How Do Copper Enzymes Hydroxylate Aliphatic Substrates? Recent Insights from the Chemistry of Model Systems
Author(s) -
Rolff Malte,
Tuczek Felix
Publication year - 2008
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.200705533
Subject(s) - hydroxylation , chemistry , copper , monooxygenase , context (archaeology) , enzyme , ligand (biochemistry) , substrate (aquarium) , model system , stereochemistry , organic chemistry , biochemistry , computational chemistry , cytochrome p450 , receptor , biology , paleontology , ecology
Copper at work : The aliphatic ligand hydroxylation by a copper–oxygen center has been observed for the first time on a model system of the enzyme PHM (peptidylglycine‐α‐hydroxylating monooxygenase). This result is put in the context of the enzymatic mechanism, which presumably involves a high‐valent copper oxo unit (violet‐red) that hydroxylates the substrate (cyan).