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.

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.

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.