Abstract
This review shortly summarizes the structural and functional properties of ceruloplasmin, the blue copper oxidase of vertebrates. Particular emphasis will be put on the unique copper stoichiometry of ceruloplasmin in comparison to all other multi-copper oxidases, and different hypotheses will be discussed to explain the apparently useless redundancy of type 1 copper ions in the vertebrate oxidase.
Keywords: CERULOPLASMIN, MULTI-COPPER OXIDASE, ascorbate oxidase (C), Coprinus cinereus laccase, ascorbate oxidase, aceruloplasminemia, Copper transport, ferroxidase, multi-copper ferroxidase
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