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  4. Artificial metalloenzymes : proteins as hosts for enantioselective catalysis
 
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Artificial metalloenzymes : proteins as hosts for enantioselective catalysis

Auteur(s)
Ward, Thomas R.
Editeur(s)
Thomas, Christophe M.
Date de parution
2005-03-10
In
Chemical Society Reviews, 2005/34/337-346
Résumé
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.
URI
https://libra.unine.ch/handle/123456789/18901
DOI
10.1039/b314695m
Autre version
http://dx.doi.org/10.1039/b314695m
Type de publication
Resource Types::text::journal::journal article
Dossier(s) à télécharger
 main article: 1_Ward_Thomas_R._-_Artificial_metalloenzymes_proteins_20060331.pdf (602.37 KB)
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