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. Mössbauer 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.
Original language | English |
---|---|
Pages (from-to) | 835-839 |
Number of pages | 5 |
Journal | Hyperfine Interactions |
Volume | 91 |
Issue number | 1 |
DOIs | |
State | Published - Dec 1994 |