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Tailoring the Active Site of Chemzymes by Using a Chemogenetic‐Optimization Procedure: Towards Substrate‐Specific Artificial Hydrogenases Based on the Biotin–Avidin Technology
Author(s) -
Klein Gérard,
Humbert Nicolas,
Gradinaru Julieta,
Ivanova Anita,
Gilardoni François,
Rusbandi Untung E.,
Ward Thomas R.
Publication year - 2005
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.200502000
Subject(s) - avidin , biotin , streptavidin , substrate (aquarium) , hydrogenase , biotinylation , selectivity , active site , combinatorial chemistry , chemistry , enzyme , biochemistry , catalysis , biology , ecology
The combination of chemical‐ with genetic‐optimization strategies (i.e. chemogenetic) allows the production of artificial hydrogenases based on the biotin–avidin technology. In the spirit of enzymes, second‐coordination‐sphere interactions between the host protein (streptavidin) and the substrate (an olefin) allow fine‐tuning of the selectivity to produce either R or S hydrogenation products.