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Last modified: 9 April 1999

Bibliography on structural studies of ferritins

    Apoferritin

  1. Aoyama, K., Ogawa, K., Kimura, Y. and Fujiyoshi, Y. (1995) A method for 2D crystallization of soluble proteins at liquid-liquid interface. Ultramicroscopy 57, 345-354.
  2. Bauminger, E.R., Harrison, P.M., Hechel, D., Nowik, I. and Treffry, A. (1991) Iron (III) can be transferred between ferritin molecules. Proc. R. Soc. Lond. B244, 211-217.
  3. Chasteen, N.D., Antanaitis, B.C. and Aisen, P. (1985) Iron deposition in apoferritin. Evidence for the formation of a mixed valence binuclear iron complex. J. Biol. Chem. 260, 2926-2929.
  4. Clerté, S., Dautant, A., d'Estaintot, B.L., Gallois, B., Mizunoe, Y., Wai, S.N. and Précigoux, G. (1999) Expression, purification, crystallization and preliminary X­ray diffraction results from Campylobacter jejuni ferritin. Acta Crystallogr. D55, 299-301.
  5. Fetter, J., Cohen, J., Danger, D., Sanders­Loehr, J. and Theil, E.C. (1997) The influence of conserved tyrosine 30 and tissue­dependent differences in sequence on ferritin function: Use of blue and purple Fe(III) species as reporters of ferroxidation. J. Biol. Inorg. Chem. 2, 652-661.
  6. Gallois, B., d'Estaintot, B.L., Michaux, M.­A., Dautant, A., Granier, T., Précigoux, G., Soruco, J.­A., Roland, F., Chavas­Alba, O., Herbas, A. and Crichton, R.R. (1997) X­ray structure of recombinant horse L­chain apoferritin at 2.0 Å resolution: Implications for stability and function. J. Biol. Inorg. Chem. 2, 360-367.
  7. Granier, T., Gallois, B., Dautant, A., d'Estaintot, B.L. and Précigoux, G. (1996) Preliminary X­ray diffraction studies of the tetragonal form of native horse­spleen apoferritin. Acta Crystallogr. D52, 594-596.
  8. Granier, T., Gallois, B., Dautant, A., d'Estaintot, B.L. and Précigoux, G. (1997) Comparison of the structures of the cubic and tetragonal forms of horse­spleen apoferritin. Acta Crystallogr. D53, 580-587.
  9. Granier, T., Comberton, G., Gallois, B., d'Estaintot, B.L., Dautant, A. and Précigoux, G. (1998) Evidence of new cadmium binding sites in recombinant horse L­chain ferritin by anomalous Fourier difference map calculation. Proteins 31, 477-485.
  10. Grant, R.A., Filman, D.J., Finkel, S.E., Kolter, R. and Hogle, J.M. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nature Struct. Biol. 5, 294-303.
  11. Ha, Y., Theil, E.C. and Allewell, N.M. (1997) Preliminary analysis of amphibian red cell M ferritin in a novel tetragonal unit cell. Acta Crystallogr. D53, 513-523.
  12. Hanna, P.M., Chen, Y. and Chasteen, N.D. (1991) Initial iron oxidation in horse spleen apoferritin. Characterization of a mixed­valence iron(II)­iron(III) complex. J. Biol. Chem. 266, 886-893.
  13. Hempstead, P.D., Hudson, A.J., Artymiuk, P.J., Andrews, S.C., Banfield, M.J., Guest, J.R. and Harrison, P.M. (1994) Direct observation of the iron binding sites in a ferritin. FEBS Lett. 350, 258-262.
  14. Hempstead, P.D., Yewdall, S.J., Fernie, A.R., Lawson, D.M., Artymiuk, P.J., Rice, D.W., Ford, G.C. and Harrison, P.M. (1997) Comparison of the three­dimensional structures of recombinant human H and horse L ferritins at high resolution. J. Mol. Biol. 268, 424-448.
  15. Ilari, A., Savino, C., Stefanini, S., Chiancone, E. and Tsernoglou, D. (1999) Crystallization and preliminary X­ray crystallographic analysis of the unusual ferritin from Listeria innocua. Acta Crystallogr. D55, 552-553.
  16. Jacobs, D., Watt, G.D., Frankel, R.B. and Papaefthymiou, G.C. (1989) Fe2+ binding to apo and holo mammalian ferritin. Biochemistry 28, 9216-9221.
  17. Lawson, D.M., Treffry, A., Artymiuk, P.J., Harrison, P.M., Yewdall, S.J., Luzzago, A., Cesareni, G., Levi, S. and Arosio, P. (1989) Identification of the ferroxidase centre in ferritin. FEBS Lett. 254, 207-210.
  18. Lawson, D.M., Artymiuk, P.J., Yewdall, S.J., Smith, J.M.A., Livingstone, J.C., Treffry, A., Luzzago, A., Levi, S., Arosio, P., Cesareni, G., Thomas, C.D., Shaw, W.V. and Harrison, P.M. (1991) Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature 349, 541-544.
  19. Levi, S., Santambrogio, P., Albertini, A. and Arosio, P. (1993) Human ferritin H­chains can be obtained in non­assembled stable forms which have ferroxidase activity. FEBS Lett. 336, 309-312.
  20. Martsev, S.P., Vlasov, A.P. and Arosio, P. (1998) Distinct stability of recombinant L and H subunits of human ferritin: calorimetric and ANS binding studies. Protein Engineering 11, 377-381.
  21. Michaux, M.A., Dautant, A., Gallois, B., Granier, T., d'Estaintot, B.L. and Précigoux, G. (1996) Structural investigation of the complexation properties between horse spleen apoferritin and metalloporphyrins. Proteins 24, 314-321.
  22. Pereira, A.S., Small, W., Krebs, C., Tavares, P., Edmondson, D.E., Theil, E.C. and Huynh, B.­H. (1998) Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization. Biochemistry 37, 9871-9876.
  23. Précigoux, G., Yariv, J., Gallois, B., Dautant, A., Courseille, C. and d'Estaintot, B.L. (1994) A crystallographic study of haem binding to ferritin. Acta Crystallogr. D50, 739-743.
  24. Sayers, D.E., Theil, E.C. and Rennick, F.J. (1983) A distinct environment for iron(III) in the complex with horse spleen apoferritin observed by x­ray absorption spectroscopy. J. Biol. Chem. 258, 14076-14079.
  25. Stefanini, S., Desideri, A., Vecchini, P., Drakenberg, T. and Chiancone, E. (1989) Identification of the iron entry channels in apoferritin. Chemical modification and spectroscopic studies. Biochemistry 28, 378-382.
  26. Sun, S. and Chasteen, N.D. (1994) Rapid kinetics of the EPR­active species formed during initial iron uptake in horse spleen apoferritin. Biochemistry 33, 15095-15102.
  27. Takagi, H., Shi, D., Ha, Y., Allewell, N.M. and Theil, E.C. (1998) Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J. Biol. Chem. 273, 18685-18688.
  28. Treffry, A., Bauminger, E.R., Hechel, D., Hodson, N.W., Nowik, I., Yewdall, S.J. and Harrison, P.M. (1993) Defining the roles of the threefold channels in iron uptake, iron oxidation and iron­core formation in ferritin: A study aided by site­directed mutagenesis. Biochem. J. 296, 721-728.
  29. Treffry, A., Zhao, Z., Quail, M.A., Guest, J.R. and Harrison, P.M. (1995) Iron(II) oxidation by H chain ferritin: evidence from site­directed mutagenesis that a transient blue species is formed at the dinuclear iron center. Biochemistry 34, 15204-15213.
  30. Treffry, A., Hawkins, C., Williams, J.M., Guest, J.R. and Harrison, P.M. (1996) Lability of iron at the dinuclear centres of ferritin studied by competition with four chelators. J. Biol. Inorg. Chem. 1, 49-60.
  31. Treffry, A., Zhao, Z., Quail, M.A., Guest, J.R. and Harrison, P.M. (1998) The use of zinc(II) to probe iron binding and oxidation by the ferritin (EcFtnA) of Escherichia coli. J. Biol. Inorg. Chem. 3, 682-688.
  32. Trikha, J., Theil, E.C. and Allewell, N.M. (1995) High resolution crystal structures of amphibian red­cell L ferritin: Potential roles for structural plasticity and solvation in function. J. Mol. Biol. 248, 949-967.
  33. Trikha, J., Waldo, G.S., Lewandowski, F.A., Ha, Y., Theil, E.C., Weber, P.C. and Allewell, N.M. (1994) Crystallization and structural analysis of bullfrog red cell L­subunit ferritins. Proteins 18, 107-118.
  34. Wade, V.J., Levi, S., Arosio, P., Treffry, A., Harrison, P.M. and Mann, S. (1991) Influence of site­directed modifications on the formation of iron cores in ferritin. J. Mol. Biol. 221, 1443-1452.
  35. Waldo, G.S., Ling, J., Sanders­Loehr, J. and Theil, E.C. (1993) Formation of an Fe(III)­tyrosinate complex during biomineralization of H­subunit ferritin. Science 259, 796-798.
  36. Wardeska, J.G., Viglione, B. and Chasteen, N.D. (1986) Metal ion complexes of apoferritin. Evidence for initial binding in the hydrophilic channels. J. Biol. Chem. 261, 6677-6683.
  37. Watt, R.K., Frankel, R.B. and Watt, G.D. (1992) Redox reactions of apo mammalian ferritin. Biochemistry 31, 9673-9679.
  38. Yang, C.Y., Meagher, A., Huynh, B.­H., Sayers, D.E. and Theil, E.C. (1987) Iron(III) clusters bound to horse spleen apoferritin: an X­ray absorption and Mössbauer spectroscopy study that shows that iron nuclei can form on the protein. Biochemistry 26, 497-503.
  39. Yang, D. and Nagayama, K. (1995) Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation. Biochem. J. 307, 253-256.
  40. Yang, D., Matsubara, K., Yamaki, M., Ebina, S. and Nagayama, K. (1994) Heterogeneities in ferritin dimers as characterized by gel filtration, nuclear magnetic resonance, electrophoresis, transmission electron microscopy, and gene engineering techniques. Biochim. Biophys. Acta 1206, 173-179.

    Iron core

  41. Baader, S.L., Bill, E., Trautwein, A.X., Bruchelt, G. and Matzanke, B.F. (1996) Mobilization of iron from cellular ferritin by ascorbic acid in neuroblastoma SK­N­SH cells: an EPR study. FEBS Lett. 381, 131-134.
  42. Bauminger, E.R., Harrison, P.M., Nowik, I. and Treffry, A. (1989) Mössbauer spectroscopic study of the initial stages of iron­core formation in horse spleen apoferritin: evidence for both isolated Fe(III) atoms and oxo­bridged Fe(III) dimers as early intermediates. Biochemistry 28, 5486-5493.
  43. Bauminger, E.R., Harrison, P.M., Hechel, D., Nowik, I. and Treffry, A. (1991) Mössbauer spectroscopic investigation of structure­function relations in ferritins. Biochim. Biophys. Acta 1118, 48-58.
  44. Bauminger, E.R., Harrison, P.M., Hechel, D., Hodson, N.W., Nowik, I., Treffry, A. and Yewdall, S.J. (1993) Iron (II) oxidation and early intermediates of iron­core formation in recombinant human H­chain ferritin. Biochem. J. 296, 709-719.
  45. Bauminger, E.R., Treffry, A., Hudson, A.J., Hechel, D., Hodson, N.W., Andrews, S.C., Levi, S., Nowik, I., Arosio, P. and Guest, J.R. (1994) Iron incorporation into ferritins: evidence for the transfer of monomeric Fe(III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia coli. Biochem. J. 302, 813-820.
  46. Bell, S.H., Weir, M.P., Dickson, D.P., Gibson, J.F., Sharp, G.A. and Peters, T.J. (1984) Mössbauer spectroscopic studies of human haemosiderin and ferritin. Biochim. Biophys. Acta 787, 227-236.
  47. Cheng, Y.G. and Chasteen, N.D. (1991) Role of phosphate in initial iron deposition in apoferritin. Biochemistry 30, 2947-2953.
  48. Dubiel, S.M., Zablotna­Rypien, B., Mackey, J.B. and Williams, J.M. (1999) Magnetic properties of human liver and brain ferritin. Eur. Biophys. J. 28, 263-267.
  49. Gider, S., Awschalom, D.D., Douglas, T., Mann, S. and Chaparala, M. (1995) Classical and quantum magnetic phenomena in natural and artificial ferritin proteins. Science 268, 77-80.
  50. Hudson, A.J., Andrews, S.C., Hawkins, C., Williams, J.M., Izuhara, M., Meldrum, F.C., Mann, S., Harrison, P.M. and Guest, J.R. (1993) Overproduction, purification and characterization of the Escherichia coli ferritin. Eur. J. Biochem. 218, 985-995.
  51. Mann, S., Bannister, J.V. and Williams, R.J.P. (1986) Structure and composition of ferritin cores isolated from human spleen, limpet (Patella vulgata) hemolymph and bacterial (Pseudomonas aeruginosa) cells. J. Mol. Biol. 188, 225-232.
  52. Mann, S., Williams, J.M., Treffry, A. and Harrison, P.M. (1987) Reconstituted and native iron­cores of bacterioferritin and ferritin. J. Mol. Biol. 198, 405-416.
  53. Mackle, P., Garner, C.D., Ward, R.J. and Peters, T.J. (1991) Iron K­edge absorption spectroscopic investigations of the cores of ferritin and haemosiderins. Biochim. Biophys. Acta 1115, 145-150.
  54. Mayer, D.E., Rohrer, J.S., Schoeller, D.A. and Harris, D.C. (1983) Fate of oxygen during ferritin iron incorporation. Biochemistry 22, 876-880.
  55. Meldrum, F.C., Heywood, B.R. and Mann, S. (1992) Magnetoferritin: in vitro synthesis of a novel magnetic protein. Science 257, 522-523.
  56. Rohrer, J.S., Joo, M.S., Dartyge, E., Sayers, D.E., Fontaine, A. and Theil, E.C. (1987) Stabilization of iron in a ferrous form by ferritin. A study using dispersive and conventional x­ray absorption spectroscopy. J. Biol. Chem. 262, 13385-13387.
  57. Rohrer, J.S., Islam, Q.T., Watt, G.D., Sayers, D.E. and Theil, E.C. (1990) Iron environment in ferritin with large amounts of phosphate, from Azotobacter vinelandii and horse spleen, analyzed using extended X­ray absorption fine structure (EXAFS). Biochemistry 29, 259-264.
  58. St. Pierre, T.G., Bell, S.H., Dickson, D.P., 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. Biochim. Biophys. Acta 870, 127-134.
  59. St. Pierre, T.G., Pollard, R.K., Dickson, D.P., Ward, R.J. and Peters, T.J. (1988) Mössbauer spectroscopic studies of deproteinised, sub­fractionated and reconstituted ferritins: the relationship between haemosiderin and ferritin. Biochim. Biophys. Acta 952, 158-163.
  60. Sasaki, Y., Suzuki, Y. and Ishibashi, T. (1994) Fluorescent X­ray interference from a protein monolayer. Science 263, 62-64.
  61. Treffry, A. and Harrison, P.M. (1979) The binding of ferric iron by ferritin. Biochem. J. 181, 709-716.
  62. Wade, V.J., Treffry, A., Laulhere, J.P., Bauminger, E.R., Cleton, M.I., Mann, S., Briat, J.F. and Harrison, P.M. (1993) Structure and composition of ferritin cores from pea seed (Pisum sativum). Biochim. Biophys. Acta 1161, 91-96.
  63. Waldo, G.S., Wright, E., Whang, Z.H., Briat, J.F., Theil, E.C. and Sayers, D.E. (1996) Formation of the ferritin iron mineral occurs in plastids. Plant Physiol. 109, 797-802.
  64. Xu, B. and Chasteen, N.D. (1991) Iron oxidation chemistry in ferritin. Increasing Fe/O2 stoichiometry during core formation. J. Biol. Chem. 266, 19965-19970.
Reviews on ferritins