Artificial metalloenzymes: proteins as hosts for enantioselective catalysis
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 116771
Author(s) Thomas, Christophe M.; Ward, Thomas R.
Author(s) at UniBasel Ward, Thomas R.
Year 2005
Title Artificial metalloenzymes: proteins as hosts for enantioselective catalysis
Journal Chemical Society Reviews
Volume 34
Number 4
Pages / Article-Number 337-46
Keywords Asymmetric synthesis and induction (enzymic; artificial metalloenzymes development for enantioselective catalysis); Enzymes Role: CAT (Catalyst use), USES (Uses) (metallo-, artificial; artificial metalloenzymes development for enantioselective catalysis); Hydrogenation (stereoselective; artificial metalloenzymes development for enantioselective hydrogenation of dehydro-amino acid derivs.); Amino acids Role: BPN (Biosynthetic preparation), BIOL (Biological study), PREP (Preparation) (unsatd., N-p
Abstract Enantioselective catalysis is one of the most efficient ways to synthesize high-added-value enantiomerically pure organic compounds. As the subtle details which govern enantioselection cannot be reliably predicted or computed, catalysis relies more and more on a combinatorial approach. Biocatalysis offers an attractive, and often complementary, alternative for the synthesis of enantiopure products. From a combinatorial perspective, the potential of directed evolution techniques in optimizing an enzyme's selectivity is unrivaled. In this review, attention is focused on the construction of artificial metalloenzymes for enantioselective catalytic applications. Such systems are shown to combine properties of both homogeneous and enzymatic kingdoms. This review also includes our recent research results and implications in the development of new semisynthetic metalloproteins for the enantioselective hydrogenation of N-protected dehydro-amino acids.
Publisher Royal Society of Chemistry
ISSN/ISBN 0306-0012 ; 1460-4744
edoc-URL http://edoc.unibas.ch/dok/A5254486
Full Text on edoc No
Digital Object Identifier DOI 10.1039/B314695M
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/15778767
ISI-Number WOS:000227764800004
Document type (ISI) Journal Article, Review
 
   

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