This article deals with tyrosinase, an enzyme that converts monophenols into diphenols and subsequently into orthoquinones with concomitant use of molecular oxygen as the source of oxygen atoms and oxidizing equivalents. The enzyme occurs widespread in nature. Its active center consists of a dinuclear copper site. The occurrence of tyrosinases and their biological function is reviewed. Information about primary (aa sequence, genetic organization), secondary, and tertiary structures is reviewed and, where appropriate, compared with similar information about related proteins with a dinuclear Cu site (hemocyanins, catechol oxidase). Methods to produce and purify tyrosinase are reviewed. Spectroscopic studies (optical; EPR, NMR, EXAFS) are reviewed in relation to the enzyme mechanism, which is discussed at the end of the article.
Structure, spectroscopy, and function of tyrosinase; comparison with hemocyanin and catechol oxidase
BUBACCO, LUIGI;
2010
Abstract
This article deals with tyrosinase, an enzyme that converts monophenols into diphenols and subsequently into orthoquinones with concomitant use of molecular oxygen as the source of oxygen atoms and oxidizing equivalents. The enzyme occurs widespread in nature. Its active center consists of a dinuclear copper site. The occurrence of tyrosinases and their biological function is reviewed. Information about primary (aa sequence, genetic organization), secondary, and tertiary structures is reviewed and, where appropriate, compared with similar information about related proteins with a dinuclear Cu site (hemocyanins, catechol oxidase). Methods to produce and purify tyrosinase are reviewed. Spectroscopic studies (optical; EPR, NMR, EXAFS) are reviewed in relation to the enzyme mechanism, which is discussed at the end of the article.Pubblicazioni consigliate
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