Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex.

@article{Prossnitz1989ReconstitutionOT,
  title={Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex.},
  author={Eric E Prossnitz and Antony Gee and Giovanna Ferro-Luzzi Ames},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 9},
  pages={5006-14}
}
The periplasmic histidine transport system of Salmonella typhimurium has been reconstituted in isolated right-side-out membrane vesicles. The reconstituted system is entirely dependent on both the periplasmic protein, HisJ, and the membrane-bound complex, composed of proteins HisQ, HisM, and HisP. Transport is also dependent on the presence of ascorbate and phenazine methosulfate, which provide the energy for transport. Ascorbate oxidation generates a proton-motive-force, which allows ATP… CONTINUE READING