Moving Fe2+ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates.

@article{Behera2014MovingFF,
  title={Moving Fe2+ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates.},
  author={Rabindra Kumar Behera and Elizabeth C. Theil},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 22},
  pages={7925-30}
}
Ferritin biominerals are protein-caged metabolic iron concentrates used for iron-protein cofactors and oxidant protection (Fe(2+) and O2 sequestration). Fe(2+) passage through ion channels in the protein cages, like membrane ion channels, required for ferritin biomineral synthesis, is followed by Fe(2+) substrate movement to ferritin enzyme (Fox) sites. Fe(2+) and O2 substrates are coupled via a diferric peroxo (DFP) intermediate, λmax 650 nm, which decays to [Fe(3+)-O-Fe(3+)] precursors of… CONTINUE READING

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