Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities.

@article{Ortenberg2003FunctionsOT,
  title={Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities.},
  author={Ron Ortenberg and Jon et Beckwith},
  journal={Antioxidants & redox signaling},
  year={2003},
  volume={5 4},
  pages={403-11}
}
A large family of enzymes contributes to the thiol-disulfide redox environment of the cells of most organisms. These proteins belong to pathways that carry out a variety of reactions, including the promotion of disulfide bond formation in extracytoplasmic proteins, the isomerization of proteins with incorrect disulfide bonds, and the reduction of disulfide bonds in the active sites of cytoplasmic proteins. Although the redox activities of these proteins measured in vitro often is consistent… CONTINUE READING