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.
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Received 19 February 2002; received after revision 29 March 2002; accepted 2 April 2002
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Bielli, P., Calabrese, L. Structure to function relationships in ceruloplasmin: a 'moonlighting' protein. CMLS, Cell. Mol. Life Sci. 59, 1413–1427 (2002). https://doi.org/10.1007/s00018-002-8519-2
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DOI: https://doi.org/10.1007/s00018-002-8519-2