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

Pordea, Anca and Ward, Thomas R.. (2008) Chemogenetic protein engineering : an efficient tool for the optimization of artificial metalloenzymes. Chemical Communications, 44 (36). pp. 4239-4249.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5254473

Downloads: Statistics Overview


A review. Artificial metalloenzymes, based on the incorporation of a catalytically active organometallic moiety within a host protein, lie at the interface between organometallic and enzymic catalysis. In terms of activity, reaction repertoire, substrate range, and operating conditions, they take advantage of the versatility of the organometallic chem. In contrast, the enantioselectivity is detd. by the biomol. scaffold, which provides a well defined 2nd coordination sphere to the organometallic moiety, reminiscent of enzymes. The attractive feature of such systems is their optimization potential, which combines chem. and genetic methods (i.e., chemogenetic) to screen diversity space. Here, the authors describe the implementation of such an optimization protocol for artificial transfer hydrogenases, for which they have the most detailed understanding. [on SciFinder(R)]
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:Royal Society of Chemistry
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:01 Dec 2016 07:26
Deposited On:22 Mar 2012 14:16

Repository Staff Only: item control page