Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase.

@article{Mohr1999NitricOS,
  title={Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase.},
  author={Susanne Mohr and Hussein Hallak and A de Boitte and Eduardo G. Lapetina and Bernhard Br{\"u}ne},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 14},
  pages={9427-30}
}
S-Nitrosylation of protein thiol groups by nitric oxide (NO) is a widely recognized protein modification. In this study we show that nitrosonium tetrafluoroborate (BF4NO), a NO+ donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S-nitrosylation and caused enzyme inhibition. The resultant protein-S-nitrosothiol was found to be unstable and to decompose spontaneously, thereby restoring enzyme activity. In contrast, the NO-releasing compound S… CONTINUE READING