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Human Carbonic Anhydrase II as Host Protein for the Creation of Artificial Metalloenzymes : the Asymmetric Transfer Hydrogenation of Imines

Monnard, Fabien W. and Nogueira, Elisa S. and Heinisch, Tillmann and Schirmer, Tilman and Ward, Thomas R.. (2013) Human Carbonic Anhydrase II as Host Protein for the Creation of Artificial Metalloenzymes : the Asymmetric Transfer Hydrogenation of Imines. Chemical Science, 4 (6). p. 3269.

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Official URL: http://edoc.unibas.ch/dok/A6212070

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Abstract

In the presence of human carbonic anhydrase II, aryl-sulfonamide-bearing IrCp* pianostool complexes catalyze the asymmetric transfer hydrogenation of imines. Critical cofactor–protein interactions revealed by the X-ray structure of [(η5-Cp*)Ir(pico 4)Cl] 9 ⊂ WT hCA II were genetically optimized to improve the catalytic performance of the artificial metalloenzyme (68% ee, kcat/KM 6.11 × 10−3 min−1 mM−1).
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Nogueira, Elisa S. and Schirmer, Tilman and Ward, Thomas R. R. and Monnard, Fabien
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Royal Society of Chemistry
ISSN:2041-6520
e-ISSN:2041-6539
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:10 Apr 2017 13:45
Deposited On:31 Jan 2014 09:50

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