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.

Determination of the iron state in ferrous iron containing vitamins and dietary supplements: application of Mössbauer spectroscopy.

Determination of the iron state in commercially manufactured iron containing vitamins and dietary supplements is important for evaluation of pharmaceuticals quality. Mössbauer (nuclear gamma-resonance) spectroscopy was used for analyzing the iron state in commercial pharmaceutical products containing ferrous fumarate (FeC(4)H(2)O(4)), ferrous sulfate (FeSO(4)), ferrous bisglycinate chelate (Ferrochel) and ferrous iron (hydrolyzed protein chelate). Mössbauer parameters and the iron states were determined for iron compounds in the studied pharmaceuticals. Various ferric and ferrous impurities were found in all of the commercial products. The quantities of ferric impurities exceeded the FDA limitation of 2% in products containing ferrous fumarate. The quantities of ferric impurities exceeded 58% and 30% in products containing ferrous bisglycinate chelate and ferrous iron (hydrolyzed protein chelate), respectively. The presence of ferrous and ferric impurities was not related to the ageing of the vitamins and dietary supplements. Two pharmaceutical products contained major iron compounds, the Mössbauer parameters of which did not correspond to the ferrous fumarate or ferrous bisglycinate chelate claimed by the manufacturer.

Hyperfine interactions in the iron cores from various pharmaceutically important iron-dextran complexes and human ferritin: a comparative study by Mössbauer spectroscopy.

Mössbauer spectroscopy has been used to study the hyperfine interactions in the iron cores of pharmaceutically important industrial and elaborated iron-dextran complexes (ferritin models) and human ferritin. Mössbauer spectra of frozen solutions and lyophilized samples of iron-dextran complexes at 87 K demonstrated magnetic, superparamagnetic and paramagnetic states of iron in various complexes. Mössbauer spectra of human ferritin in frozen solution and lyophilized form showed paramagnetic state of iron at 87 K. Small variations of Mössbauer hyperfine parameters were observed for different samples at 87 and 295 K, respectively, supposing the homogenous iron cores. The values of quadrupole splitting for iron-dextran complexes and ferritin in frozen solutions at 87 K varied from 0.639 to 0.744 mm/s while those of lyophilized samples at 87 K varied from 0.714 to 0.788 mm/s. The values of quadrupole splitting for iron-dextran complexes and ferritin in lyophilized form at 295 K varied from 0.687 to 0.741 mm/s. The values of hyperfine magnetic fields on the 57Fe nuclei in several iron-dextran complexes at 87 K varied from approximately 231 to approximately 485 kOe. These small variations of the hyperfine parameters were related to several types of the hydrous iron oxide microstructural modifications in the core and variations of the iron core size. The influence of lyophilization on the iron core structure was also assumed. In addition, Mössbauer spectra were evaluated in supposition of heterogeneous iron core in all samples.

Characterization of the heme iron in pyridoxylated hemoglobin cross-linked by glutaraldehyde using Mössbauer spectroscopy.

The heme iron in human adult hemoglobin modified by both pyridoxal-5'-phosphate and glutaraldehyde was characterized by Mössbauer spectroscopy and compared with non-modified hemoglobin. Mössbauer spectra of the samples were measured at 87 and 295 K (1yophilized form) and at 87 K (frozen solution). The values of quadrupole splitting for the oxy-form of modified hemoglobin were found to be lower than those of the oxy-form of hemoglobin without modifications in lyophilized form and frozen solution, respectively. On the other hand, the values of quadrupole splitting for the deoxy-form of modified and non-modified hemoglobins in frozen solution were the same. The Mössbauer spectra of the oxy-form of modified hemoglobin were also analyzed in terms of the heme iron non-equivalence in alpha- and beta-subunits of tetramer. The differences of the tendencies of temperature dependencies of quadrupole splitting for the oxy-form of modified and non-modified hemoglobins in lyophilized form were shown. These results indicated that the heme iron electronic structure and stereochemistry were changed in the oxy-form of pyridoxylated hemoglobin cross-linked by glutaraldehyde.