Issue 36, 2008

Chemogenetic protein engineering: an efficient tool for the optimization of artificial metalloenzymes

Abstract

Artificial metalloenzymes, based on the incorporation of a catalytically active organometallic moiety within a host protein, lie at the interface between organometallic and enzymatic catalysis. In terms of activity, reaction repertoire, substrate range and operating conditions, they take advantage of the versatility of the organometallic chemistry. In contrast, the enantioselectivity is determined by the biomolecular scaffold, which provides a well defined second coordination sphere to the organometallic moiety, reminiscent of enzymes. The attractive feature of such systems is their optimization potential, which combines chemical and genetic methods (i.e. chemogenetic) to screen diversity space. This feature article describes the implementation of such an optimization protocol for artificial transfer hydrogenases, for which we have the most detailed understanding.

Graphical abstract: Chemogenetic protein engineering: an efficient tool for the optimization of artificial metalloenzymes

Article information

Article type
Feature Article
Submitted
21 Apr 2008
Accepted
11 Jun 2008
First published
12 Aug 2008

Chem. Commun., 2008, 4239-4249

Chemogenetic protein engineering: an efficient tool for the optimization of artificial metalloenzymes

A. Pordea and T. R. Ward, Chem. Commun., 2008, 4239 DOI: 10.1039/B806652C

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