Abstract
Tyrosinase is a copper containing monooxygenase catalyzing the formation of melanin pigments and other polyphenolic compounds from various phenols. This review deals with the recent progress on the molecular structure of the enzyme from Neurospora crassa and the unique features of the binuclear active site copper complex involved in the activation of molecular oxygen and the binding of substrates. The results of the spectroscopic properties of Neurospora tyrosinase will also be discussed in the light of the structural similarity of the copper complex in the oxygen binding hemocyanins.
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