Biometals

, Volume 17, Issue 3, pp 197–202

Iron and proteins for iron storage and detoxification

Authors

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

DOI: 10.1023/B:BIOM.0000027692.24395.76

Cite this article as:
Chiancone, E., Ceci, P., Ilari, A. et al. Biometals (2004) 17: 197. doi:10.1023/B:BIOM.0000027692.24395.76

Abstract

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)ferritiniron storage-detoxification
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© Kluwer Academic Publishers 2004