Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.

@article{Rouhier2004PoplarPQ,
  title={Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.},
  author={Nicolas Rouhier and Eric Gelhaye and Jos{\'e} M. Gualberto and Marie-Noelle Jordy and Elisabeth De Fay and Masakazu Hirasawa and S{\'e}bastien Duplessis and St{\'e}phane D. Lemaire and Pascal Frey and Francis Martin and Wanda Manieri and David B. Knaff and Jean-Pierre Jacquot},
  journal={Plant physiology},
  year={2004},
  volume={134 3},
  pages={1027-38}
}
Peroxiredoxins are ubiquitous thioredoxin- or glutaredoxin-dependent peroxidases, the function of which is to destroy peroxides. Peroxiredoxin Q, one of the four plant subtypes, is a homolog of the bacterial bacterioferritin comigratory proteins. We show here that the poplar (Populus tremula x Populus tremuloides) protein acts as a monomer with an intramolecular disulfide bridge between two conserved cysteines. A wide range of electron donors and substrates was tested. Unlike type II… CONTINUE READING