Design of artificial metalloenzymes

Thomas, Christophe M. and Ward, Thomas R.. (2005) Design of artificial metalloenzymes. Applied Organometallic Chemistry, 19 (1). pp. 35-39.

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Official URL: http://edoc.unibas.ch/dok/A5254487

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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.
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
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:24 Apr 2017 13:46
Deposited On:22 Mar 2012 14:07

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