Jump to main content
Jump to site search

Issue 7, 2015
Previous Article Next Article

Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding

Author affiliations

Abstract

As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (kcat 7.8 × 10−2 s−1, KM 1.1 × 10−5 M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu·6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate.

Graphical abstract: Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding

Back to tab navigation

Supplementary files

Publication details

The article was received on 24 Mar 2015, accepted on 07 May 2015 and first published on 07 May 2015


Article type: Edge Article
DOI: 10.1039/C5SC01065A
Author version
available:
Download author version (PDF)
Citation: Chem. Sci., 2015,6, 4060-4065
  • Open access: Creative Commons BY license
  •   Request permissions

    Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding

    N. Fujieda, J. Schätti, E. Stuttfeld, K. Ohkubo, T. Maier, S. Fukuzumi and T. R. Ward, Chem. Sci., 2015, 6, 4060
    DOI: 10.1039/C5SC01065A

    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.

Search articles by author

Spotlight

Advertisements