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 ferr
ihydrite nucleation. Mossbauer spectroscopic studies of recombinant H-
chain ferritins show the following: (1) fast Fe2+ oxidation is associa
ted with the formation of Fe3+ dimers at the ferroxidase centre; (2) w
ithin 30 min, a portion of the dimers have split to Fe3+ monomers and
some monomers have moved to the threefold channels; (3) over longer ti
mes, a trend dimer --> monomer --> core is established. Core formation
is accelerated if L chains are present.