Structure to function relationships in ceruloplasmin: a 'moonlighting' protein |
| |
Authors: | Bielli P Calabrese L |
| |
Institution: | (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.at, AT;(2) Department of Biochemical Sciences, University of Rome 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome (Italy), IT |
| |
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.
Received 19 February 2002; received after revision 29 March 2002; accepted 2 April 2002
RID="*"
ID="*"Corresponding author. |
| |
Keywords: | , Ceruloplasmin, multicopper oxidase, moonlighting protein, iron metabolism, copper metabolism, electron transfer, |
本文献已被 PubMed SpringerLink 等数据库收录! |
|