Evidence for proton shuffling in a thioredoxin-like protein during catalysis.

@article{Narzi2008EvidenceFP,
  title={Evidence for proton shuffling in a thioredoxin-like protein during catalysis.},
  author={Daniele Narzi and Shirley W. I. Siu and Christian U. Stirnimann and John P. A. Grimshaw and Rudi Glockshuber and Guido Capitani and Rainer A. B{\"o}ckmann},
  journal={Journal of molecular biology},
  year={2008},
  volume={382 4},
  pages={
          978-86
        }
}
Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in substrate proteins both in prokaryotic and in eukaryotic cells. All members of the Trx family with thiol-disulfide oxidoreductase activity contain the characteristic Cys-X-X-Cys motif in their active site. Here, using Poisson-Boltzmann-based protonation-state calculations based on 100-ns molecular dynamics simulations, we investigate the catalytic mechanism of DsbL, the most oxidizing… CONTINUE READING
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