Hyperfine interactions in soybean and lupin oxy-leghemoglobins studied using Mössbauer spectroscopy with a high velocity resolution

A comparative study of monomeric soybean and lupin leghemoglobins in the oxy-form was carried out using Mossbauer spectroscopy with a high velocity resolution at 90 K. The 57Fe hyperfine parameters of measured spectra were evaluated and compared with possible structural differences in the heme Fe(II)–O 2 bond.