Biophysical characterization of the MerP-like amino-terminal extension of the mercuric reductase from Ralstonia metallidurans CH34

@article{Rossy2003BiophysicalCO,
  title={Biophysical characterization of the MerP-like amino-terminal extension of the mercuric reductase from Ralstonia metallidurans CH34},
  author={Emmanuel Rossy and Ludovic Champier and Beate Bersch and Bernhard Brutscher and Martin Blackledge and Jacques Cov{\'e}s},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2003},
  volume={9},
  pages={49-58}
}
The purified native mercuric reductase (MerA) from Ralstonia metallidurans CH34 contains an N-terminal sequence of 68 amino acids predicted to be homologous to MerP, the periplasmic mercury-binding protein. This MerP-like protein has now been expressed independently. The protein was named MerAa by homology with Ccc2a, the first soluble domain of the copper-transporting ATPase from yeast. Δa has been characterized using a set of biophysical techniques. The binding of mercury was followed using… CONTINUE READING