How Do Copper Enzymes Hydroxylate Aliphatic Substrates? Recent Insights from the Chemistry of Model Systems | Zendy

Rolff Malte | Zendy; Tuczek Felix | Zendy

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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).

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