, Volume 17, Issue 3, pp 197–202 | Cite as

Iron and proteins for iron storage and detoxification

  • Emilia Chiancone
  • Pierpaolo Ceci
  • Andrea Ilari
  • Frederica Ribacchi
  • Simonetta Stefanini


Iron is required by most organisms, but is potentially toxic due to the low solubility of the stable oxidation state, Fe(III), and to the tendency to potentiate the production of reactive oxygen species, ROS. The reactivity of iron is counteracted by bacteria with the same strategies employed by the host, namely by sequestering the metal into ferritin, the ubiquitous iron storage protein. Ferritins are highly conserved, hollow spheres constructed from 24 subunits that are endowed with ferroxidase activity and can harbour up to 4500 iron atoms as oxy-hydroxide micelles. The release of the metal upon reduction can alter the microorganism-host iron balance and hence permit bacteria to overcome iron limitation. In bacteria, the relevance of the Dps (DNA-binding proteins from starved cells) family in iron storage-detoxification has been recognized recently. The seminal studies on the protein from Listeria innocua demonstrated that Dps proteins have ferritin-like activity and most importantly have the capacity to attenuate the production of ROS. This latter function allows bacterial pathogens that lack catalase, e.g. Porphyromonas gingivalis, to survive in an aerobic environment and resist to peroxide stress.

Dps proteins (DNA-binding proteins from starved cells) ferritin iron storage-detoxification 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Almiron M, Link AJ, Furlong D, Kolter R. 1992 A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6, 2646-2654.PubMedGoogle Scholar
  2. Altuvia S, Almiron M, Huisman G, Kolter R, Storz G. 1994 The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase. Mol Microbiol 13, 265-272.PubMedGoogle Scholar
  3. Andrews SC. 1998 Iron storage in bacteria. Adv Microb Physiol 40, 281-351.PubMedGoogle Scholar
  4. Bou-Abdallah F, Lewin AC, Le Brun NE, Moore GR, Chasteen ND. 2002 Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry. J Biol Chem 277, 37064-37069.PubMedGoogle Scholar
  5. Bozzi M, Mignogna G, Stefanini S, Barra D, Longhi C, Valenti P, Chiancone E. 1997 A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua J Biol Chem 272, 3259-3265.PubMedGoogle Scholar
  6. Ceci P, Ilari A, Falvo E, Chiancone E. 2003 The Dps protein of Agrobacterium tumefaciens does not bind to DNA, but protects it towards oxidative cleavage. X-ray crystal structure, iron binding and hydroxyl-radical scavenging properties. J Biol Chem 278, 20319-20326.PubMedGoogle Scholar
  7. Cheesman M et al.1993 Haem and non-haem iron sites in Escherichia coli bacterioferritin: spectroscopic and model building studies. Biochem J 292, 47-56.PubMedGoogle Scholar
  8. Cornelissen CN, Sparling PF 1994 Iron piracy: acquisition of transferrin-bound iron by bacterial pathogens. Mol Microbiol 14, 843-50.PubMedGoogle Scholar
  9. Deneer HG, Healey V, Boycluk I. 1995 Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp. Microbiology 141, 1985-1992.PubMedGoogle Scholar
  10. Douglas T, Ripoli DR 1998 Calculated electrostatic gradients in recombinant human H-chain ferritin. Protein Sci 7, 1083-91.PubMedGoogle Scholar
  11. Frolow F, Kalb AJ (Gilboa), Yariv J. 1994 Structure of a unique twofold symmetric haem-binding site. Nat Struct Biol 1, 453-460.PubMedGoogle Scholar
  12. Grant RA, Filman DJ, Finkel SE, Kolter R, Hogle JM 1998 The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat Struct Biol 5, 294-302.PubMedGoogle Scholar
  13. Harrison PM, Arosio P. 1996 The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275, 161-203.PubMedGoogle Scholar
  14. Ilari A, Stefanini S, Chiancone E, Tsernoglou D 2000 The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat Struct Biol 7, 38-43.PubMedGoogle Scholar
  15. Ishikawa T, Mizunoe Y, Kawabata S, Takade A, Harada M, Wai SN, Yoshida S. 2003 The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J Bacteriol 185, 1010-1017.PubMedGoogle Scholar
  16. Johnson WL, Varner L, Poch M. 1991 Acquisition of iron by Legionella pneumophila: role of iron reductase. Infect Immun 59, 2376-2381.PubMedGoogle Scholar
  17. Jones T, Spencer R, Walsh C. 1978 Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues. Biochemistry 19, 4011-4017.Google Scholar
  18. Papinutto E, Dundon WG, Pitulis N, Battistutta R, Montecucco C, Zanotti G. 2002 Structure of two iron-binding proteins from Bacillus anthracis. J Biol Chem 277, 15093-15098.PubMedGoogle Scholar
  19. Schryvers AB, Stojilijkovic I. 1999 Iron acquisition systems in the pathogenic Neisseria. Mol Microbiol 32, 1117-1123.PubMedGoogle Scholar
  20. Takagi H, Shi D, Ha Y, Allewell NM, Theil EC. 1998 Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J Biol Chem 273, 18685-18688.PubMedGoogle Scholar
  21. Tonello F, Dundon WG, Satin B, Molinari M, Tognon G, Grandi G, Del Giudice G, Rappuoli R, Montecucco C. 1999 The Helicobacter pylori neutrophil-activating protein is an iron-binding protein with dodecameric structure. Mol Microbiol 34, 238-246.PubMedGoogle Scholar
  22. Ueshima J, Shoji M, Ratnayake DB, Abe K, Yoshida S, Yamamoto K, Nakayama K. 2003 Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect Immun 71, 1170-1178.PubMedGoogle Scholar
  23. Wandersman C, Stojilijkovic I. 2000 Bacterial heme sources: the role of heme, hemporotein receptors and hemophores Curr Opin Microbiol 3, 215-220.PubMedGoogle Scholar
  24. Yamamoto Y, Poole LB, Hantgan RR, Kamio Y. 2002 An ironbinding protein, Dpr, from Streptococcus mutans prevents irondependent hydroxyl radical formation in vitro. J Bacteriol 184, 2931-2939.PubMedGoogle Scholar
  25. Yang X, Chen-Barret Y, Arosio P, Chasteen ND. 1998 Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins. Biochemistry 37, 9743-9750.PubMedGoogle Scholar
  26. Zhao G, Ceci P, Ilari A, Giangiacomo L, Laue TM, Chiancone E, Chasteen ND. 2002 Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritinlike DNA-binding protein of Escherichia coli. J Biol Chem 277, 27689-27696.PubMedGoogle Scholar
  27. Zhao G, Bou-Abdallah F, Arosio P, Levi S, Janus-Chandler C, Chasteen ND. 2003 Multiple pathways for mineral core formation in mammalian apoferritin. The role of hydrogen peroxide. Biochemistry 18, 3142-3150.Google Scholar

Copyright information

© Kluwer Academic Publishers 2004

Authors and Affiliations

  • Emilia Chiancone
    • 1
  • Pierpaolo Ceci
    • 1
  • Andrea Ilari
    • 1
  • Frederica Ribacchi
    • 1
  • Simonetta Stefanini
    • 1
  1. 1.CNR Institute of Molecular Biology and Pathology, Department of Biochemical SciencesUniversity of Rome `La Sapienza'RomeItaly

Personalised recommendations