Abstract
Ferritin stores iron as ferrihydrite inside a shell composed of H and L protein chains. H chains contain ferroxidase centres catalysing Fe2+ oxidation, while L chains lack these centres but seem to promote ferrihydrite nucleation. Mossbauer spectroscopic studies of recombinant H-chain ferritins show the following: (1) fast Fe2+ oxidation is associated with the formation of Fe3+ dimers at the ferroxidase centre; (2) within 30 min, a portion of the dimers have split to Fe3+ monomers and some monomers have moved to the threefold channels; (3) over longer times, a trend dimer → monomer → core is established. Core formation is accelerated if L chains are present.
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