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Mössbauer spectroscopic studies of the cores of human, limpet and bacterial ferritins

St Pierre, T.G., Bell, S.H., Dickson, D.P.E., Mann, S., Webb, J., Moore, G.R. and Williams, R.J.P. (1986) Mössbauer spectroscopic studies of the cores of human, limpet and bacterial ferritins. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 870 (1). pp. 127-134.

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Ferritin cores from human spleen, limpet (Patella vulgata) haemolymph and bacterial (Pseudomonasaeruginosa) cells have been investigated using 57Fe Mössbauer spectroscopy. The Mössbauer spectra were recorded over a range of temperatures from 1.3 to 78 K. At 78 K, all the spectra are quadrupole-split doublets with similar quadrupole splittings and isomer shifts, characteristic of iron(III), while at sufficiently low temperatures the spectra of all the samples show well-resolved magnetic splitting. At intermediate temperatures, the spectra from the human ferritin exhibit typical superparamagnetic behaviour, while those from the bacterial ferritin show behaviour corresponding to a transition from a magnetically ordered to a paramagnetic state. The spectra from the limpet ferritin show a complex combination of the two effects. The results are discussed in terms of the magnetic behaviour of small particles. The data are consistent with magnetic ordering temperatures of about 3 and 30 K for the bacterial and limpet ferritin cores, respectively, while the data indicate that the magnetic ordering temperature for the human ferritin cores must be above 50 K. These differences are interpreted as being related to different densities of iron in the cores and to variations in the composition of the cores. The human ferritin cores are observed to have a mean superparamagnetic blocking temperature of about 40 K, while that of the limpet ferritin cores is about 25 K. This difference is interpreted as being due not only to different mean numbers of iron atoms in the two types of core but also to the higher degree of crystallinity in the cores of the human ferritin.

Item Type: Journal Article
Murdoch Affiliation(s): School of Mathematical and Physical Sciences
Publisher: Elsevier
Copyright: 1986 Elsevier Science Publishers B.V.
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