57Fe quadrupole splitting and isomer shift in various oxyhemoglobins: study using Mössbauer spectroscopy

Abstract

A comparative study of normal human, rabbit and pig oxyhemoglobins and oxyhemoglobin from patients with chronic myeloleukemia and multiple myeloma using Mössbauer spectroscopy with a high velocity resolution demonstrated small variations of the 57 Fe quadrupole splitting and isomer shift. These variations may be a result of small structural differences in the heme iron stereochemistry of various hemoglobins.

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.…”

57Fe enrichment in mice for β-thalassaemia studies via Mössbauer spectroscopy of blood samples

“…This doublet was fitted with two different sub-doublets indicating the αand β-globins of haemoglobin's tetramer (denoted as Hb-α and Ηb-β, respectively). Note that, in other studies, two doublets were also used to describe the oxy-haemoglobin in spectra from blood samples of humans and animals (Hoy et al 1986;Oshtrakh and Semionkin 1986;Oshtrakh et al 2010).…”

“…Mössbauer spectroscopy was previously utilized to study iron complexes in blood and organs of humans and some animals. Two doublets were used to describe the oxyhaemoglobin in MS spectra of blood samples from human and animals (Hoy et al 1986;Oshtrakh and Semionkin 1986;Oshtrakh et al 2010). When spectra from RCBs of healthy people and patients with thalassaemia were compared, a new component was identified in the patient spectra which was considered to be ferritin-like iron (Xuanhui et al 1988;Abreu et al 1989;Jiang et al 1994).…”