Possibilities of Mössbauer spectroscopy with a high velocity resolution in studying small variations in 57Fe hyperfine parameters of iron-containing proteins

Abstract

The possibilities of Mossbauer spectroscopy with a high velocity resolution in investigating small variations in the 57Fe hyperfine parameters of iron-containing proteins are demonstrated. Differences of quadrupole splitting for human and rabbit oxyhemoglobins were observed. Variations of quadrupole splitting and isomer shift for human liver ferritin and its model Imferon were revealed. Small differences in these parameters were also found for iron-storage proteins in normal chicken liver and spleen tissues and in such tissues from chickens with lymphoid leukemia.