edoc-vmtest

Artificial metalloenzymes for enantioselective catalysis based on biotin-avidin

Collot, Jerome and Gradinaru, Julieta and Humbert, Nicolas and Skander, Myriem and Zocchi, Andrea and Ward, Thomas R.. (2003) Artificial metalloenzymes for enantioselective catalysis based on biotin-avidin. Journal of the American Chemical Society, 125 (30). pp. 9030-9031.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5254438

Downloads: Statistics Overview

Abstract

Homogeneous and enzymatic catalysis offer complementary means to generate enantiomerically pure compounds. Incorporation of achiral biotinylated rhodium−diphosphine complexes into (strept)avidin yields artificial metalloenzymes for the hydrogenation of N-protected dehydroamino acids. A chemogenetic optimization procedure allows one to produce (R)-acetamidoalanine with 96% enantioselectivity. These hybrid catalysts display features reminiscent both of enzymatic and of homogeneous systems.
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:American Chemical Society
ISSN:0002-7863
e-ISSN:1520-5126
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:24 Apr 2017 14:03
Deposited On:22 Mar 2012 14:06

Repository Staff Only: item control page