Cellular and Molecular Life Sciences CMLS

, Volume 59, Issue 9, pp 1413–1427 | Cite as

Structure to function relationships in ceruloplasmin: a 'moonlighting' protein

  • P. Bielli
  • L. Calabrese

Abstract.

Specialised copper sites have been recruited during evolution to provide long-range electron transfer reactivity and oxygen binding and activation in proteins destined to cope with oxygen reactivity in different organisms. Ceruloplasmin is an ancient multicopper oxidase evolved to insure a safe handling of oxygen in some metabolic pathways of vertebrates. The presently available knowledge of its structure provides a glimpse of its plasticity, revealing a multitude of binding sites that point to an elaborate mechanism of multifunctional activity. Ceruloplasmin represents an example of a 'moonlighting' protein that overcomes the one gene-one structure-one function concept to follow the changes of the organism in its physiological and pathological conditions.

Key words. Ceruloplasmin; multicopper oxidase; moonlighting protein; iron metabolism; copper metabolism; electron transfer. 

Copyright information

© Birkhäuser Verlag, 2002

Authors and Affiliations

  • P. Bielli
    • 1
  • L. Calabrese
    • 2
  1. 1.Institute of Microbiology and Genetics, Vienna Biocenter, University of Vienna, Dr. Bohrgasse 9/4, 1030 Vienna (Austria), Fax + 43 1 42779546, e-mail: pamela@gem.univie.ac.atAT
  2. 2.Department of Biochemical Sciences, University of Rome 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome (Italy)IT

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