Structure to function relationships in ceruloplasmin

A 'moonlighting' protein

P. Bielli, L. Calabrese

Research output: Contribution to journalArticle

157 Citations (Scopus)

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 structureone function concept to follow the changes of the organism in its physiological and pathological conditions.

Original languageEnglish
Pages (from-to)1413-1427
Number of pages15
JournalCellular and Molecular Life Sciences
Volume59
Issue number9
DOIs
Publication statusPublished - Sep 2002

Fingerprint

Ceruloplasmin
Oxygen
Safe handling
Proteins
Metabolic Networks and Pathways
Plasticity
Vertebrates
Copper
Oxidoreductases
Genes
Chemical activation
Binding Sites
Electrons

Keywords

  • Ceruloplasmin
  • Copper metabolism
  • Electron transfer
  • Iron metabolism
  • Moonlighting protein
  • Multicopper oxidase

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology

Cite this

Structure to function relationships in ceruloplasmin : A 'moonlighting' protein. / Bielli, P.; Calabrese, L.

In: Cellular and Molecular Life Sciences, Vol. 59, No. 9, 09.2002, p. 1413-1427.

Research output: Contribution to journalArticle

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