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The catalytic core of tyrosinase is composed of H 2 L 2 tetramer, and its active center contains binuclear copper ions, which form a six-coordinated chelating structure through His61, His85, His94(CuA), His259, His263 and His296(CuB) ( 2+ is the key step to catalyze the oxidation of L-tyrosine to dopaquinone, which depends on the precise regulation of the hydrophobic environment in the active chamber ( CuA and CuB are connected by an oxygen bridge to form a rigid structure, required for catalytic activity

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It distinguishes carefully between well-supported observations and areas where the evidence is thin or absent