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Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein

Ward, Thomas R.. (2005) Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein. Chemistry - A European Journal, 11 (13). pp. 3798-3804.

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Official URL: http://edoc.unibas.ch/dok/A5254497

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Abstract

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.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:0947-6539
e-ISSN:1521-3765
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:24 Apr 2017 13:52
Deposited On:22 Mar 2012 14:07

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