Different Properties of Ferrous Iron in Deoxygenated Hemoglobin Chains
نویسندگان
چکیده
— Iron 57-enriched, deoxygenated human (adult) hemoglobin (HbA), its isolated asHand /?sn-chains, and the partially iron 57-enriched, fully functional hemoglobin a2(Fe) j82(Fe) were investigated by Mossbauer spectroscopy in the temperature range 4.2 K-200 K. According to our experimental accuracy ( ± 0.006 mm s) the temperature dependent quadrupole splittings &EQ(T) of deoxygenated HbA, <XSHand ^sH-chains are not identical from about 100K down to 4.2 K, and A£Q of HbA is not the average value of the AEVvalues of the isolated chains. The quadrupole splitting of a2(Fe) /?2(Fe) turns out to be practically the same as that of HbA. These findings are also reflected by the isomershifts. Line widths are comparable for all compounds.
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