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Dynamics of Iron in Ferritin

  • E. R. Bauminger
  • I. Nowik
  • P. M. Harrison
  • A. Treffry
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 1)

Abstract

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.

Keywords

Iron Atom Iron Core Spectral Area Protein Shell Iron Nucleus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    E.R. Bauminger, S.G. Cohen, I. Nowik, S. Ofer, and J. Yariv, Proc. Natl. Acad. Sci. (U.S.) 80, 736 (1983) I. Nowik, E.R. Bauminger, S.G. Cohen, and S. Ofer, Phys. Rev. A 31, 2291 (1985). E.W. Knapp, E.W. Fischer, and F. Parak, J. Chem. Phys. 78, 4701 (1983)..CrossRefGoogle Scholar
  2. 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

Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • E. R. Bauminger
    • 1
  • I. Nowik
    • 1
  • P. M. Harrison
    • 2
  • A. Treffry
    • 2
  1. 1.Racah Institute of PhysicsThe Hebrew UniversityJerusalemIsrael
  2. 2.Department of BiochemistryThe University of SheffieldSheffieldUK

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