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Metallochaperones & Metal Ion Homeostasis

  1. Valeria C. Culotta

Published Online: 15 DEC 2011

DOI: 10.1002/9781119951438.eibc0258

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Culotta, V. C. 2011. Metallochaperones & Metal Ion Homeostasis. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. Johns Hopkins University Bloomberg School of Public Health, Baltimore, MD, USA

Publication History

  1. Published Online: 15 DEC 2011


There exists a large array of proteins that rely on metal ions such as copper and manganese for function and these so-called metalloproteins are housed in diverse locations throughout the cell. It is imperative that each metalloprotein connects with the proper metal ion and also at the right time. How does this meeting of protein and metal occur in a specific and regulated fashion? The problem seems paramount when one considers the potentially toxic nature of metals. With the harm that metals can impose on biomolecules, these ions are never allowed to roam freely in the reactive form and, as such, the bioavailability of metals within cells is very limited. To overcome this problem, eukaryote cells have evolved with specific ‘metal trafficking pathways’ or designated routes a metal ion can follow once inside the cell. On one hand, the bulk of the metal may be subject to a dead fate involving sequestration by metal detoxification systems. On the other hand, a fraction of the metal destined for metalloproteins enters a trafficking pathway that involves both membrane transporters and ‘metal chaperones’ that directly insert the metal into the target metalloprotein. The bulk of current knowledge on metal chaperones and metal trafficking pathways has emerged from studies on copper and to a lesser degree on manganese. The work described herein focuses on paradigms developed for copper and manganese, with possible implications for other essential metals as well.


  • copper;
  • manganese;
  • SOD1;
  • SOD2;
  • mitochondria;
  • Golgi;
  • chaperones;
  • transporters;
  • cytochrome c oxidase;
  • CCS;
  • ATX1