Jump to main content
Jump to site search

Issue 1, 2015
Previous Article Next Article

Novel artificial metalloenzymes by in vivo incorporation of metal-binding unnatural amino acids

Author affiliations

Abstract

Artificial metalloenzymes have emerged as an attractive new approach to enantioselective catalysis. Herein, we introduce a novel strategy for preparation of artificial metalloenzymes utilizing amber stop codon suppression methodology for the in vivo incorporation of metal-binding unnatural amino acids. The resulting artificial metalloenzymes were applied in catalytic asymmetric Friedel–Crafts alkylation reactions and up to 83% ee for the product was achieved.

Graphical abstract: Novel artificial metalloenzymes by in vivo incorporation of metal-binding unnatural amino acids

Back to tab navigation

Supplementary files

Article information


Submitted
23 May 2014
Accepted
09 Oct 2014
First published
09 Oct 2014

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2015,6, 770-776
Article type
Edge Article
Author version available

Novel artificial metalloenzymes by in vivo incorporation of metal-binding unnatural amino acids

I. Drienovská, A. Rioz-Martínez, A. Draksharapu and G. Roelfes, Chem. Sci., 2015, 6, 770
DOI: 10.1039/C4SC01525H

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

Reproduced material should be attributed as follows:

  • For reproduction of material from NJC:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
  • For reproduction of material from PCCP:
    [Original citation] - Published by the PCCP Owner Societies.
  • For reproduction of material from PPS:
    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
  • For reproduction of material from all other RSC journals:
    [Original citation] - Published by The Royal Society of Chemistry.

Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.


Social activity

Search articles by author

Spotlight

Advertisements