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. 1977 Sep 28;3(3-4):229-38.
doi: 10.1007/BF00535698.

Investigation of two deoxygenated haemoglobin-haptoglobin complexes by Mössbauer spectroscopy

A Alfsen, D Bade, U Bürck, H Eicher, S Formanek, G M Kalvius, F Lavialle, A Mayer, F Parak, J Tejada, U F Thomanek

Investigation of two deoxygenated haemoglobin-haptoglobin complexes by Mössbauer spectroscopy

A Alfsen et al. Biophys Struct Mech. .

Abstract

Haemoglobin Haptoglobin complexes formed when [Hp+]/[Hb]= 1/1 and [Hp]/[Hb] =2/1 were investigated by 57Fe Mössbauer spectroscopy. Both samples gave a spectrum consisting of a single quadrupole doublet. The temperature dependence of the quadrupole splitting was also identical for both samples. This proves that in both samples the nearest neighbour environment of the iron atom must be the same. A comparison with earlier investigations on myoglobin and haemoglobin indicates that the electronic structure of iron in the HbHp-complexes is similar to that in myoglobin.

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