Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone

@inproceedings{Dow2014CharacterizationOA,
  title={Characterization of a periplasmic nitrate reductase in complex with its biosynthetic chaperone},
  author={Jennifer M. Dow and Sabine Grahl and Richard Ward and Rachael A. Evans and Olwyn Byron and David G Norman and Tracy Palmer and Frank Sargent},
  booktitle={The FEBS journal},
  year={2014}
}
Escherichia coli is a Gram-negative bacterium that can use nitrate during anaerobic respiration. The catalytic subunit of the periplasmic nitrate reductase NapA contains two types of redox cofactor and is exported across the cytoplasmic membrane by the twin-arginine protein transport pathway. NapD is a small cytoplasmic protein that is essential for the activity of the periplasmic nitrate reductase and binds tightly to the twin-arginine signal peptide of NapA. Here we show, using spin labelling… CONTINUE READING
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