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Issue 8, 2013
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Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines

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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 cofactorprotein 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


Submitted
22 Apr 2013
Accepted
31 May 2013
First published
12 Jun 2013

Chem. Sci., 2013,4, 3269-3274
Article type
Edge Article

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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