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Improving the enantioselectivity of artificial transfer hydrogenases based on the biotin-streptavidin technology by combinations of point mutations

Pordea, Anca and Creus, Marc and Letondor, Christophe and Ivanova, Anita and Ward, Thomas R.. (2010) Improving the enantioselectivity of artificial transfer hydrogenases based on the biotin-streptavidin technology by combinations of point mutations. Inorganica Chimica Acta, 363 (3). pp. 601-604.

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Official URL: http://edoc.unibas.ch/dok/A5841541

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Abstract

Artificial metalloenzymes based on the incorporation of biotinylated ruthenium piano-stool complexes within streptavidin can be readily optimized by chemical or genetic means. We performed genetic modifications of such artificial metalloenzymes for the transfer hydrogenation of aromatic ketones, by combining targeted point mutations of the host protein. Upon using the P64G-L124V double mutant of streptavidin in combination with the [eta(6)-(p-cymene)Ru(Biot-p-L)Cl] complex, the enantioselectivity can be increased up to 98% ee (R) for the reduction of p-methylacetophenone, which is the highest selectivity obtained up to date with an artificial transfer hydrogenase. (C) 2009 Elsevier B.V. All rights reserved.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Creus, Marc and Ward, Thomas R. R.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Elsevier
ISSN:0020-1693
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:24 Apr 2017 10:17
Deposited On:14 Sep 2012 06:55

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