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Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein
Author(s) -
Ward Thomas R.
Publication year - 2005
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200401232
Subject(s) - enantiopure drug , biotinylation , enantioselective synthesis , catalysis , avidin , selectivity , chemistry , combinatorial chemistry , rhodium , streptavidin , artificial enzyme , enzyme catalysis , biocatalysis , organic chemistry , biotin , reaction mechanism , biochemistry
Enzymatic and homogeneous catalysis offer complementary means to produce enantiopure products. Incorporation of achiral, biotinylated aminodiphosphine–rhodium complexes in (strept)avidin affords enantioselective hydrogenation catalysts. A combined chemogenetic procedure allows the optimization of the activity and the selectivity of such artificial metalloenzymes: the reduction of acetamidoacrylate proceeds to produce N ‐acetamidoalanine in either 96 % ee ( R ) or 80 % ee ( S ). In addition to providing a chiral second coordination sphere and, thus, selectivity to the catalyst, the phenomenon of protein‐accelerated catalysis (e.g., increased activity) was unraveled. Such artificial metalloenzymes based on the biotin–avidin technology display features that are reminiscent of both homogeneous and of enzymatic catalysis.