Study of human, rabbit and pig oxyhemoglobins using high velocity resolution Mössbauer spectroscopy in relation to their structural and functional variations

Differences of the 57 Fe hyperfine parameters in both oxyhemoglobin and spleen from normal human and patient with primary myelofibrosis

“…These spectra were fitted using two models (see [10][11][12]17]): 1) equivalent Fe(II) electron structure in α-and β-subunits of HbO 2 with spectra fitting using one quadrupole doublet; 2) non-equivalent Fe(II) electron structure in α-and β-subunits of HbO 2 with spectra fitting using two quadrupole doublets with equal areas. It should be noted that in the spectrum of normal human RBC an additional minor component 3 (S ∼ 5 %) with parameters similar to carboxyhemoglobin (HbCO) was observed.…”

“…An increase in velocity resolution in Mössbauer spectroscopy permits to achieve better adjusting to resonance, more precise spectra measurement with decrease in instrumental error on velocity scale and better fit of complicated spectra due to increase in spectral points number (see [5][6][7][8][9]). New studies of normal HbO 2 with different molecular structure and HbO 2 from patients with blood system malignant diseases as well as chicken liver and spleen tissues with increased velocity resolution demonstrated some small differences in the 57 Fe hyperfine parameters [8,[10][11][12]. To continue these studies we chose a case with a very rare blood system malignant disease named primary myelofibrosis (PMF).…”

Mössbauer spectroscopy with a high velocity resolution: Advances in biomedical, pharmaceutical, cosmochemical and nanotechnological research

“…Further results were obtained in the study of normal oxyhemoglobin in red blood cells from normal adult human, rabbit and pig as well as oxyhemoglobin in red blood cells from patients with chronic myeloleukemia and multiple myeloma [18][19][20]. Mössbauer spectra were measured at 90 K in 4096 channels and then converted into 1024 channels due to a low iron content (see spectra of rabbit oxyhemoglobin and oxyhemoglobin from patient with chronic myeloleukemia in Fig.…”

The 57Fe hyperfine interactions in the life sciences: application of Mössbauer spectroscopy with a high velocity resolution in the study of iron-containing biomolecules and pharmaceutical compounds

“…To analyze the effect of subtle stereochemical differences in the heme Fe(II) environment related to the variations in the primary protein structure on the heme Fe(II) electronic structure we applied Mössbauer spectroscopy with a high velocity resolution for the study of tetrameric normal human, rabbit and pig hemoglobins and monomeric soybean a and lupin I leghemoglobins [38][39][40][41][42]. Human, rabbit and pig red blood cells (RBC) were twice washed from blood by centrifugation in physiological solution.…”

“…Oxy-leghemoglobins were in solution with 100 mM phosphate buffer at pH 7. About 2.5 ml of each leghemoglobin solution was immediately frozen with liquid nitrogen and stored at 77 K. Details of hemoglobins preparation can be found in [38][39][40][41][42] and references therein. Mössbauer spectra of tetrameric rabbit hemoglobin and monomeric soybean leghemoglobin in the oxy-form measured at 90 K are shown in Fig.…”