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Significance How ions move between ion channel exits and final destinations is poorly understood. Fe2+ substrate enters ferritin protein nanocages through cage-penetrating ion channels analogous to membrane ion channels. Fe2+ then moves to ferritin cage enzyme (Fox ) sites, reacting with oxygen substrate to produce diferric oxy complexes, the precursors of ferritin minerals (Fe2 O3 ⋅H2 O). Ferritin iron is used in heme and iron–sulfur cofactors. Monitoring rapid (ms) diferric peroxo formation in WT ferritin and E57 and E136 variants showed that these conserved residues are required for enzyme activity. Combining the results with older structural studies identifies ferritin E57 and E136 links in the Fe2+ bucket brigade connecting ferritin ion channels and destinations. By analogy, key carboxylates in ion transporters link ion channels to cytoplasmic destinations.

Moving Fe 2+ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates

Moving Fe ²⁺ from ferritin ion channels to catalytic OH centers depends on conserved protein cage carboxylates