On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily.

@article{Debarbieux2000OnTF,
  title={On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily.},
  author={Laurent Debarbieux and Jonathan Beckwith},
  journal={Journal of bacteriology},
  year={2000},
  volume={182 3},
  pages={723-7}
}
Escherichia coli thioredoxin 1 has been characterized in vivo and in vitro as one of the most efficient reductants of disulfide bonds. Nevertheless, under some conditions, thioredoxin 1 can also act in vivo as an oxidant, promoting formation of disulfide bonds in the cytoplasm (E. J. Stewart, F. Aslund, and J. Beckwith, EMBO J. 17:5543-5550, 1998). We recently showed that when a signal sequence is attached to thioredoxin 1 it is exported to the periplasm, where it can also act as an oxidant… CONTINUE READING

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