Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 116741
Author(s) Letondor, Christophe; Humbert, Nicolas; Ward, Thomas R.
Author(s) at UniBasel Ward, Thomas R.
Year 2005
Title Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation
Journal Proceedings of the National Academy of Sciences
Volume 102
Number 13
Pages / Article-Number 4683-7
Keywords second coordination sphere, asymmetric catalysis, chemzymes
Abstract Most physiological and biotechnological processes rely on molecular recognition between chiral (handed) molecules. Manmade homogeneous catalysts and enzymes offer complementary means for producing enantiopure (single-handed) compounds. As the subtle details that govern chiral discrimination are difficult to predict, improving the performance of such catalysts often relies on trial-and-error procedures. Homogeneous catalysts are optimized by chemical modification of the chiral environment around the metal center. Enzymes can be improved by modification of gene encoding the protein. Incorporation of a biotinylated organometallic catalyst into a host protein (avidin or streptavidin) affords versatile artificial metalloenzymes for the reduction of ketones by transfer hydrogenation. The boric acid·formate mixture was identified as a hydrogen source compatible with these artificial metalloenzymes. A combined chemo-genetic procedure allows us to optimize the activity and selectivity of these hybrid catalysts: up to 94% (R) enantiomeric excess for the reduction of p-methylacetophenone. These artificial metalloenzymes display features reminiscent of both homogeneous catalysts and enzymes.
Publisher National Academy of Sciences
ISSN/ISBN 1091-6490
edoc-URL http://edoc.unibas.ch/dok/A5254457
Full Text on edoc No
Digital Object Identifier DOI 10.1073/pnas.0409684102
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/15772162
ISI-Number WOS:000228074000007
Document type (ISI) Journal Article
 
   

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