Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold "ferritin-like" pores.

@article{Bellapadrona2009IronTI,
  title={Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold "ferritin-like" pores.},
  author={Giuliano Bellapadrona and Simonetta Stefanini and Carlotta Zamparelli and Elizabeth C. Theil and Emilia Chiancone},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 28},
  pages={19101-9}
}
Elucidating pore function at the 3-fold channels of 12-subunit, microbial Dps proteins is important in understanding their role in the management of iron/hydrogen peroxide. The Dps pores are called "ferritin-like" because of the structural resemblance to the 3-fold channels of 24-subunit ferritins used for iron entry and exit to and from the protein cage. In ferritins, negatively charged residues lining the pores generate a negative electrostatic gradient that guides iron ions toward the… CONTINUE READING