JBIC Journal of Biological Inorganic Chemistry

, Volume 11, Issue 7, pp 803–810

Ferritins: iron/oxygen biominerals in protein nanocages

  • Elizabeth C. Theil
  • Manolis Matzapetakis
  • Xiaofeng Liu
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DOI: 10.1007/s00775-006-0125-6

Cite this article as:
Theil, E.C., Matzapetakis, M. & Liu, X. J Biol Inorg Chem (2006) 11: 803. doi:10.1007/s00775-006-0125-6

Abstract

Ferritin protein nanocages that form iron oxy biominerals in the central nanometer cavity are nature’s answer to managing iron and oxygen; gene deletions are lethal in mammals and render bacteria more vulnerable to host release of antipathogen oxidants. The multifunctional, multisubunit proteins couple iron with oxygen (maxi-ferritins) or hydrogen peroxide (mini-ferritins) at catalytic sites that are related to di-iron sites oxidases, ribonucleotide reductase, methane monooxygenase and fatty acid desaturases, and synthesize mineral precursors. Gated pores, distributed symmetrically around the ferritin cages, control removal of iron by reductants and chelators. Gene regulation of ferritin, long known to depend on iron and, in animals, on a noncoding messenger RNA (mRNA) structure linked in a combinatorial array to functionally related mRNA of iron transport, has recently been shown to be linked to an array of proteins for antioxidant responses such as thioredoxin and quinone reductases. Ferritin DNA responds more to oxygen signals, and ferritin mRNA responds more to iron signals. Ferritin genes (DNA and RNA) and protein function at the intersection of iron and oxygen chemistry in biology.

Keywords

Iron and oxygen Ferritin RNA DNA Peroxide 

Copyright information

© SBIC 2006

Authors and Affiliations

  • Elizabeth C. Theil
    • 1
    • 2
  • Manolis Matzapetakis
    • 1
  • Xiaofeng Liu
    • 1
  1. 1.CHORI (Children’s Hospital Research Institute Oakland)OaklandUSA
  2. 2.Department of Nutritional Science and ToxicologyUniversity of California at BerkeleyBerkeleyUSA

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