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Bibliography on structural studies of bacterioferritin (cytochrome b1)

  1. Cheesman, M.R., Thomson, A.J., Greenwood, C., Moore, G.R. and Kadir, F.H. (1990) Bis­methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa. Nature 346, 771-773.
  2. Cheesman, M.R., Kadir, F.H., al­Basseet, J., al­Massad, F., Farrar, J., Greenwood, C., Thomson, A.J. and Moore, G.R. (1992) E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii. Biochem. J. 286, 361-367.
  3. Cheesman, M.R., Le Brun, N.E., Kadir, F.H., Thomson, A.J., Moore, G.R., Andrews, S.C., Guest, J.R., Harrison, P.M., Smith, J.M.A. and Yewdall, S.J. (1993) Haem and non­haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies. Biochem. J. 292, 47-56.
  4. Dautant, A., Meyer, J.­B., Yariv, J., Précigoux, G., Sweet, R., Kalb (Gilboa), A.J. and Frolow, F. (1998) Structure of a monoclinic crystal form of cytochrome b1 (bacterioferritin) from E. coli. Acta Crystallogr. D54, 16-24.
  5. Frolow, F., Kalb (Gilboa), A.J. and Yariv, J. (1993) Location of haem in bacterioferritin of E. coli. Acta Crystallogr. D49, 597-600.
  6. Frolow, F., Kalb (Gilboa), A.J. and Yariv, J. (1994) Structure of a unique twofold symmetric haem­binding site. Nature Struct. Biol. 1, 453-460.
  7. Huang, H., Zhang, F., Xu, L., Lin, Q., Huang, J. and Ding, Z. (1998) Spectroelectrochemical investigation of Azotobacter vinelandii bacterial ferritin. Bioelectrochem. Bioenergetics 44, 301-307.
  8. Kadir, F.H. and Moore, G.R. (1990) Bacterial ferritin contains 24 haem groups. FEBS Lett. 271, 141-143.
  9. Keech, A.M., Le Brun, N.E., Wilson, M.T., Andrews, S.C., Moore, G.R. and Thomson, A.J. (1997) Spectroscopic studies of cobalt(II) binding to Escherichia coli bacterioferritin. J. Biol. Chem. 272, 422-429.
  10. Le Brun, N.E., Cheesman, M.R., Thomson, A.J., Moore, G.R., Andrews, S.C., Guest, J.R. and Harrison, P.M. (1993a) An EPR investigation of non­haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate. A study using nitric oxide as a spin probe. FEBS Lett. 323, 261-266.
  11. Le Brun, N.E., Wilson, M.T., Andrews, S.C., Guest, J.R., Harrison, P.M., Thomson, A.J. and Moore, G.R. (1993b) Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin. FEBS Lett. 333, 197-202.
  12. Le Brun, N.E., Andrews, S.C., Moore, G.R. and Thomson, A.J. (1997) Interaction of nitric oxide with non­haem iron sites of Escherichia coli bacterioferritin: Reduction of nitric oxide to nitrous oxide and oxidation of iron(II) to iron(III). Biochem. J. 326, 173-179.
  13. 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.
  14. Ringeling, P.L., Davy, S.L., Monkara, F.A., Hunt, C., Dickson, D.P., McEwan, A.G. and Moore, G.R. (1994) Iron metabolism in Rhodobacter capsulatus. Characterisation of bacterioferritin and formation of non­haem iron particles in intact cells. Eur. J. Biochem. 223, 847-855.
  15. Smith, J.M.A., Ford, G.C., Harrison, P.M., Yariv, J. and Kalb (Gilboa), A.J. (1989) Molecular size and symmetry of the bacterioferritin of Escherichia coli. X­ray crystallographic characterization of four crystal forms. J. Mol. Biol. 205, 465-467.
Reviews on ferritins