Structural variations of the iron cores in human liver ferritin and its pharmaceutically important models: A comparative study using Mössbauer spectroscopy with a high velocity resolution

A comparative study of a human liver ferritin and its pharmaceutically important models Imferon, Maltofer® and Ferrum Lek using 57Fe Mössbauer spectroscopy with a high velocity resolution was performed at 295 and 90 K. Mössbauer spectra were analyzed using two models viz. homogeneous and heterogeneous, and were fitted with one or various number of doublets, respectively. Small variations of Mössbauer hyperfine parameters were revealed for these samples with both models as well as a different number of quadrupole doublets for the best spectra fit was needed in the heterogeneous model. The results were related to structural differences of the iron cores in the human liver ferritin, Imferon, Maltofer® and Ferrum Lek.