Issue 8, 2013
From the journal:

Chemical Science

Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines†

Fabien W. Monnard,a   Elisa S. Nogueira,a   Tillmann Heinisch,ab   Tilman Schirmerb  and  Thomas R. Ward*a  

* Corresponding authors

a Department of Chemistry, University of Basel, Spitalstrasse 51, CH-4056 Basel, Switzerland
E-mail: thomas.ward@unibas.ch
Fax: +41 61 267 10 05
Tel: +41 61 267 10 04

b Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland
E-mail: tilman.schirmer@unibas.ch
Fax: +41 61 267 21 09
Tel: +41 61 267 20 89

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).

Graphical abstract: Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines

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Article information

DOI
https://doi.org/10.1039/C3SC51065D
Article type
Edge Article
Submitted
22 Apr 2013
Accepted
31 May 2013
First published
12 Jun 2013

Chem. Sci., 2013,4, 3269-3274

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Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines

F. W. Monnard, E. S. Nogueira, T. Heinisch, T. Schirmer and T. R. Ward, Chem. Sci., 2013, 4, 3269 DOI: 10.1039/C3SC51065D

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