Glutathionylation of the iron superoxide dismutase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis.

@article{Castellano2008GlutathionylationOT,
  title={Glutathionylation of the iron superoxide dismutase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis.},
  author={Immacolata Castellano and Maria Rosaria Ruocco and Francesca Cecere and Antimo Di Maro and Angela Nebbioso and Andzelika Michniewicz and Giuseppe Parlato and Mariorosario Masullo and Emmanuele De Vendittis},
  journal={Biochimica et biophysica acta},
  year={2008},
  volume={1784 5},
  pages={816-26}
}
Our previous work showed that the adduct between beta-mercaptoethanol and the single cysteine residue (Cys57) in superoxide dismutase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis (PhSOD) reduces the enzyme inactivation by peroxynitrite. In this work, immunoblotting experiments prove that peroxynitrite inactivation of PhSOD involves formation of nitrotyrosine residue(s). In order to study the role of Cys57 as a redox-sensor residue modifiable by cellular thiols, a… CONTINUE READING