Investigation of two deoxygenated haemoglobin-Haptoglobin complexes by Mössbauer spectroscopy

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

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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.

Original languageEnglish
Pages (from-to)229-238
Number of pages10
JournalBiophysics of Structure and Mechanism
Volume3
Issue number3-4
DOIs
StatePublished - Sep 1977

Keywords

  • Haemoglobin
  • Haptoglobin
  • Mössbauer spectroscopy

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