Dynamics of Iron in Ferritin
It is now well established that Mossbauer spectra of Fe57 in proteins above a criticial temperature have a special shape, composed of narrow and broad absorption lines. This shape has been explained in terms of bounded diffusive motion of the iron nuclei, reflecting the motion of the protein to which the iron is attached(1). Detailed Mossbauer studies of Fe57 in the iron storage protein, ferritin, reveal a significant difference in the dynamic behaviour of iron in ferritin filled with a small number of Fe atoms per apoferritin molecule and in ferritin with an almost full iron core.
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- 2.G.C. Ford, P.M. Harrison, D.W. Rice, J.M.A. Smith, A. Treffry, J.L. White, and J. Yariv, Phil. Trans. R. Soc. Lond. B304 551 (1984).Google Scholar