I. V. Alenkina

Mössbauer spectroscopy with a high velocity resolution in the study of iron-containing proteins and model compounds.

Mössbauer spectroscopy with a high velocity resolution was used for comparative studies of human adult, rabbit and pig oxyhemoglobins, human liver ferritin and its pharmaceutically important models Imferon and Maltofer(®) as well as liver and spleen tissues from normal and lymphoid leukemia chicken. These studies revealed small variations of Mössbauer hyperfine parameters which were related to small variations of iron electronic structure and stereochemistry in these samples.

Comparative study of the iron cores in human liver ferritin, its pharmaceutical models and ferritin in chicken liver and spleen tissues using Mössbauer spectroscopy with a high velocity resolution

Application of Mössbauer spectroscopy with a high velocity resolution (4096 channels) for comparative analysis of iron cores in a human liver ferritin and its pharmaceutically important models Imferon, Maltofer(®) and Ferrum Lek as well as in iron storage proteins in chicken liver and spleen tissues allowed to reveal small variations in the (57)Fe hyperfine parameters related to differences in the iron core structure. Moreover, it was shown that the best fit of Mössbauer spectra of these samples required different number of components. The latter may indicate that the real iron core structure is more complex than that following from a simple core-shell model. The effect of different living conditions and age on the iron core in chicken liver was also considered.

57Fe Mössbauer spectroscopy and electron paramagnetic resonance studies of human liver ferritin, Ferrum Lek and Maltofer®

A human liver ferritin, commercial Ferrum Lek and Maltofer® samples were studied using Mössbauer spectroscopy and electron paramagnetic resonance. Two Mössbauer spectrometers have been used: (i) a high velocity resolution (4096 channels) at 90 and 295K, (ii) and a low velocity resolution (250 channels) at 20 and 40 K. It is shown that the three studied materials have different superparamagnetic features at various temperatures. This may be caused by different magnetic anisotropy energy barriers, sizes (volume), structures and compositions of the iron cores. The electron paramagnetic resonance spectra of the ferritin, Ferrum Lek and Maltofer® were decomposed into multiple spectral components demonstrating the presence of minor ferro- or ferrimagnetic phases along with revealing marked differences among the studied substances. Mössbauer spectroscopy provides evidences on several components in the measured spectra which could be related to different regions, layers, nanocrystallites, etc. in the iron cores that coincides with heterogeneous and multiphase models for the ferritin iron cores.

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

The 57Fe hyperfine interactions are the useful source of information about the finest structural peculiarities in various iron-containing proteins which can be essential in the natural variety of structure and function relationship in normal biomolecules as well as in its changes in the case of molecular pathology. Mössbauer spectroscopy with a high velocity resolution as the most sensitive probe for the 57Fe hyperfine interactions demonstrates some advances in the study of various hemoglobins, ferritins and pharmaceutical products that can bring new information for the life sciences.

Different 57Fe microenvironments in the nanosized iron cores in human liver ferritin and its pharmaceutical analogues on the basis of temperature dependent Mössbauer spectroscopy

Mössbauer spectra of human liver ferritin and its pharmaceutical analogues Ferrum Lek and Maltofer® measured at various temperatures within the range of 295-83K were fitted using five quadrupole doublets related to different 57Fe microenvironments in various layers/regions of the ferrihydrite and akaganéite iron cores. The observed anomalous temperature dependences of some Mössbauer parameters were considered as a result of low temperature structural rearrangements in different layers/regions in the iron core.

Comparative study of nanosized iron cores in human liver ferritin and its pharmaceutically important models Maltofer® and Ferrum Lek using Mössbauer spectroscopy

Studies of human liver ferritin and its pharmaceutically important models Maltofer® and Ferrum Lek were carried out using Mössbauer spectroscopy with a high velocity resolution at 295 and 90 K and Mössbauer spectroscopy with a low velocity resolution at 40 and 20 K. The Mössbauer spectra fits using a multi-component model confirm the hypothesis of the complicated heterogeneous structure of nanosized iron cores in the investigated samples.

An analysis of the features of the Mössbauer spectra of soybean leghemoglobin a in oxyand deoxy-forms in relation to protein structure

An analysis of the Mössbauer spectra of soybean leghemoglobin a in both oxyand deoxy-forms measured with a high velocity resolution at 90 K was carried out in comparison with the room temperature Mössbauer spectrum of the standard absorber sodium nitroprusside. On the basis of the observed features of the spectral line shapes the soybean leghemoglobin a Mössbauer spectra were fitted using two quadrupole doublets for protein oxy-form and three quadrupole doublets for protein deoxy-form. These spectral components were related to two conformational states of His E7 imidazole ring in the distal heme side and three conformational states of His F8 imidazole ring in the proximal heme side for soybean leghemoglobin a oxyand deoxy-forms, respectively.

Iron in spleen and liver: Some cases of normal tissues and tissues from patients with hematological malignancies

Iron deposits in spleen and liver tissues obtained from several healthy people and patients with mantle cell lymphoma, acute myeloid leukemia and primary myelofibrosis were studied using Mossbauer spectroscopy and magnetization measurements. The results obtained demonstrated differences in the iron content in tissues as well as some variations in the ferrihydrite-like iron core structure in the iron storage proteins in these tissues. The presence of tiny amount of magnetite and paramagnetic component in spleen and liver tissue was also detected in different quantities in the studied tissues.

Evaluation of the Debye temperature for iron cores in human liver ferritin and its pharmaceutical analogue, Ferrum Lek, using Mössbauer spectroscopy.

An iron-polymaltose complex, Ferrum Lek, used as antianemic drug and considered as a ferritin analogue and human liver ferritin were investigated in the temperature range of 295-90K using (57)Fe Mössbauer spectroscopy with a high velocity resolution (in 4096 channels). This study aimed to make a comparison of the Fe atom dynamics in the Ferrum Lek and ferritin iron cores by means of evaluation of the Debye temperature using the temperature dependence of the spectral center shift obtained with two different fitting procedures and the second order Doppler shift approach. The Debye temperature, evaluated as ΘD=502±24K for Ferrum Lek and ΘD=461±16K for human liver ferritin, demonstrated a very small difference in the Fe atom vibrations, reflecting a slightly smaller rigidity in the iron cores in human liver ferritin.

Comparative analysis of the heme iron electronic structure and stereochemistry in tetrameric rabbit hemoglobin and monomeric soybean leghemoglobin a using Mössbauer spectroscopy with a high velocity resolution

A comparative study of tetrameric rabbit hemoglobin and monomeric soybean leghemoglobin a in the oxy- and deoxy-forms was carried out using 57Fe Mössbauer spectroscopy with a high velocity resolution in order to analyze the heme iron electronic structure and stereochemistry in relation to the Mössbauer hyperfine parameters. The Mössbauer spectra of tetrameric rabbit hemoglobin in both forms were fitted using two quadrupole doublets related to the 57Fe in ɑ- and β-subunits. In contrast, the Mössbauer spectra of monomeric soybean leghemoglobin a were fitted using: (i) two quadrupole doublets for the oxy-form related to two conformational states of the distal His E7 imidazole ring and different hydrogen bonding of oxygen molecule in the oxy-form and (ii) using three quadrupole doublets for deoxy-form related to three conformational states of the proximal His F8 imidazole ring. Small variations of Mössbauer hyperfine parameters related to small differences in the heme iron electronic structure and stereochemistry in tetrameric rabbit hemoglobin and monomeric soybean leghemoglobin a are discussed.