Abstract

The existence of natural peroxiredoxin-glutaredoxin hybrid enzymes in several bacteria is in line with previous findings indicating that poplar peroxiredoxin II can use glutaredoxin as an electron donor. This peroxiredoxin remains however unique since it also uses thioredoxin with a quite good efficiency. Based on the existing fusions, we have created artificial enzymes containing a poplar peroxiredoxin module linked to glutaredoxin or thioredoxin modules. The recombinant fusion enzymes folded properly into non-covalently bound homodimers or homotetramers. Two of the three protein constructs exhibit peroxidase activity, a reaction where the two modules need to function together, but they also display enzymatic activities specific of each module. In addition, mass spectrometry analyses indicate that the Prx module can be both glutathiolated or overoxidized in vitro. This is discussed in the light of the Prx reactivity. (c) 2006 Elsevier Inc. All rights reserved

Published in

Biochemical and Biophysical Research Communications
2006, Volume: 341, number: 4, pages: 1300-1308
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE

SLU Authors

• Wingsle, Gunnar

  • Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Forest Science


Publication identifier

DOI: https://doi.org/10.1016/j.bbrc.2006.01.099

Permanent link to this page (URI)

https://res.slu.se/id/publ/11035