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

Normal human adult, rabbit and pig oxyhemoglobins in frozen red blood cell solutions were studied using Mössbauer spectroscopy with a high velocity resolution. Spectra were analyzed using two models with and without accounting for the heme iron electronic structure non-equivalence in α- and β-subunits of tetrameric hemoglobins. The observed differences of Mössbauer hyperfine parameters were related to structural variations in human, rabbit and pig oxyhemoglobins as well as to the differences in ligand binding affinities of these proteins.