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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This work was supported by the “Deutsche Forschungsgemeinschaft...
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Alfsen, A., Bade, D., van Bürck, U. et al. Investigation of two deoxygenated haemoglobin-Haptoglobin complexes by Mössbauer spectroscopy. Biophys. Struct. Mechanism 3, 229–238 (1977). https://doi.org/10.1007/BF00535698
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DOI: https://doi.org/10.1007/BF00535698