Abstract
Iron(III) monomers, dimers and clusters have been identified by Mössbauer spectroscopy during the initial stages of iron incorporation into ferritins, following Fe(II) oxidation. Iron(III) monomers seem to arise from dimer dissociation. Some of the monomers are transferred from iron poor to iron rich ferritin molecules, where they join the iron core clusters. Horse spleen ferritin, several variants of human H chain ferritin and Escherichia coli ferritin (Ec-FTN) can all accept the iron from human H chain ferritin. The small iron cores of Ec-FTN are different from those of mammalian ferritins, which indicates that the structure of the iron core depends on the protein shell.
Original language | English |
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Pages (from-to) | 237-241 |
Number of pages | 5 |
Journal | Journal of Radioanalytical and Nuclear Chemistry |
Volume | 190 |
Issue number | 2 |
DOIs | |
State | Published - Mar 1995 |