Abstract
Application of Mössbauer spectroscopy with a high velocity resolution for study different hemoglobins, ferritin, its models and chicken liver and spleen as well as normal and lymphoid chicken spleen demonstrated revealing of small variations of hyperfine parameters related to small variations of iron stereochemistry in biomolecules. These data demonstrate that Mössbauer spectroscopy with a high velocity resolution may be useful in biomedical research to distinguish small variations of iron-containing proteins in normal and pathological cases.
Highlights
Mössbauer spectroscopy is a powerful tool which allows us to observe the hyperfine splitting of the nuclear energy levels as well as changes of energies of the ground and excited states of Mössbauer nuclei in the absorption or emission spectrum of γ-rays
The simplest way to demonstrate possibilities of Mössbauer spectroscopy in revealing of small variations of the hyperfine parameters may be performed using the simplest fitting of measured spectra
Mössbauer hyperfine parameters for the spectra of both oxyhemoglobins presented in 512 channels and in 1024 channels are shown in the plot of quadrupole splitting and isomer shift (Fig. 1(c))
Summary
Mössbauer spectroscopy is a powerful tool which allows us to observe the hyperfine splitting of the nuclear energy levels as well as changes of energies of the ground and excited states of Mössbauer nuclei (for instance, 57Fe, 119Sn, 197Au and some other) in the absorption or emission spectrum of γ-rays (detailed description of the Mössbauer effect see, for instance, in [1,2,3,16]). Mössbauer spectroscopy appeared to be useful for studying so-called “drastic” and “small” changes of the iron electronic structure [6,8,9]. “Drastic” changes imply a change of the valence and/or spin state of iron resulting from the transformation or destruction of proteins In this case Mössbauer spectra or subspectra may be well defined. “Small” changes imply a change of the iron electronic structure without any change of the valence and spin state resulting from structural modifications of protein. The study of “small” changes is more complicated and requires a high precision, sensitive and stable Mössbauer spectrometer These structural modifications may be related to protein heterogeneity and functional variety in different organs, in human and various animals as well as in normal and pathological subjects due to their specific structure–function relationship. In this work we demonstrate these possibilities in revealing small variations in various iron-containing species in recent biomedical research
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