Spectroscopic studies on the binding of iron, terbium, and zinc by apoferritin.
Ultraviolet difference spectroscopy has been used to study Fe (III)-apoferritin complexes formed after addition of Fe (II) to apoferritin in air. At constant iron, the recorded spectra varied with time after Fe (II) addition and with the number of iron atoms/molecule (protein concentration). The results indicate that after production of an initial complex, rearrangement or migration of Fe (III) atoms occurs, with polynuclear species forming as end-product, probably by hydrolytic polymerization. The presence of Tb3+ or Zn2+ ions affected the Fe (III) spectra and their development in different ways. The combined data suggest that more than one site, or processes, are involved in ferritin iron-core formation and that some of the metal sites are clustered.
D000818:Animals; D001052:Apoferritins / Q000378:metabolism*; D003124:Colorimetry; D005293:Ferritins / Q000031:analogs & derivatives*; D006736:Horses; D007501:Iron / Q000378:metabolism*; D010084:Oxidation-Reduction; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013154:Spleen / Q000378:metabolism; D013725:Terbium / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
D013725:Terbium; D005293:Ferritins; D001052:Apoferritins; D007501:Iron; D015032:Zinc