Abstract
An analysis of the Mossbauer 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 Mossbauer spectrum of the standard absorber sodium nitroprusside. On the basis of the observed features of the spectral line shapes the soybean leghemoglobin a Mossbauer 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.
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