AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase.

@article{Poole2000AhpFAO,
  title={AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase.},
  author={Leslie B. Poole and C. Michael Reynolds and Zachary A Wood and P. Andrew Karplus and Holly R Ellis and M Li Calzi},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 20},
  pages={6126-33}
}
A group of bacterial flavoproteins related to thioredoxin reductase contain an additional approximately 200-amino-acid domain including a redox-active disulfide center at their N-termini. These flavoproteins, designated NADH:peroxiredoxin oxidoreductases, catalyze the pyridine-nucleotide-dependent reduction of cysteine-based peroxidases (e.g. Salmonella typhimurium AhpC, a member of the peroxiredoxin family) which in turn reduce H2O2 or organic hydroperoxides. These enzymes catalyze rapid… CONTINUE READING