ABSTRACT
Multi-copper blue oxidases are enzymes widely spread in bacteria, fungi, plants, and animals that catalyze the four-electron reduction of dioxygen to water through four sequential single-electron oxidation events of a substrate [14,140]. They contain at least one blue copper center and a trinuclear center composed by a type 2 and a type 3 copper site, and all the hitherto characterized enzymes are glycosylated. The three currently well-defined members of this family are laccase (Lc), ascorbate oxidase (AO), and ceruloplasmin (Cp).
