Sammanfattning

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

Publicerad i

Biochemical and Biophysical Research Communications
2006, Volym: 341, nummer: 4, sidor: 1300-1308
Utgivare: ACADEMIC PRESS INC ELSEVIER SCIENCE

SLU författare

• Wingsle, Gunnar

  • Institutionen för skoglig genetik och växtfysiologi, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Skogsvetenskap


Publikationens identifierare

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

Permanent länk till denna sida (URI)

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