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The amino scid sequence of Rhus vernicifera laccase was determined startion from the isolation of mRNA's followed by the PCR amplification of the cDNA fragment encoding laccase.The amino acid sequence of the tree laccase was compared with those of laccases from microorganisms and witht hose of other related multicopper oxidases including bilirubin oxidase etc. Differing from microorganism laccases the type 1 Cu of the tree laccase was found to be four-coordinated including Met. The dour-electron reduction process of bilirubin oxidase was studied with the comparison of the reaction by the laccase,giving the hydroxyl radial species as the three-electron reduced from of dioxygen.