Jump to main content
Jump to site search

Issue 8, 2013
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 22 Apr 2013, accepted on 31 May 2013 and first published on 12 Jun 2013


Article type: Edge Article
DOI: 10.1039/C3SC51065D
Citation: Chem. Sci., 2013,4, 3269-3274
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements