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Design of artificial metalloenzymes
Author(s) -
Thomas Christophe M.,
Ward Thomas R.
Publication year - 2005
Publication title -
applied organometallic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.53
H-Index - 71
eISSN - 1099-0739
pISSN - 0268-2605
DOI - 10.1002/aoc.726
Subject(s) - chemistry , biotinylation , covalent bond , catalysis , enantioselective synthesis , combinatorial chemistry , avidin , homogeneous , enzyme catalysis , enzyme , group 2 organometallic chemistry , organic chemistry , nanotechnology , molecule , biochemistry , physics , materials science , thermodynamics
Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. For this reason, in a biomimetic spirit, efforts are currently under way in different groups to design artificial enzymes. Two complementary strategies are possible to incorporate active organometallic catalyst precursors into a protein environment. The first strategy utilizes covalent anchoring of the organometallic complexes into the protein environment. The second strategy relies on the use of non‐covalent incorporation of the organometallic precursor into the protein. In this review, attention is focused on the use of semisynthetic enzymes to produce efficient enantioselective hybrid catalysts for a given reaction. This article also includes our recent research results and implications in developing the biotin–avidin technology to localize the biotinylated organometallic catalyst precursor within a well‐defined protein environment. Copyright © 2005 John Wiley & Sons, Ltd.