期刊
FEBS LETTERS
卷 -, 期 -, 页码 -出版社
WILEY
DOI: 10.1002/1873-3468.14503
关键词
catechol oxidase; coupled binuclear copper; melanin; monooxygenase; monooxygenation mechanism; tyrosinase
资金
- U.S. National Institutes of Health [DK31450]
Tyrosinase, a member of the CBC protein family, has been studied extensively. Recent research has revealed the structure of a catalytic ternary intermediate and proposed a revised mechanism for monophenol monooxygenation. These findings are significant for understanding structure-function relationships in CBC enzymes and the activation of O-2 in bioinorganic active sites.
Tyrosinase is the most predominant member of the coupled binuclear copper (CBC) protein family. The recent trapping and spectroscopic definition of the elusive catalytic ternary intermediate (enzyme/O-2/monophenol) of tyrosinase dictates a monooxygenation mechanism that revises previous proposals and involves cleavage of the mu-eta(2):eta(2)-peroxide dicopper(II) O-O bond to accept the phenolic proton, followed by monophenolate coordination to copper concomitant with aromatic hydroxylation by the non-protonated mu-oxo. Here, we compare and contrast previously proposed and current mechanistic models for monophenol monooxygenation of tyrosinase. Next, we discuss how these recent insights provide new opportunities towards uncovering structure-function relationships in CBC enzymes, as well as understanding fundamental principles for O-2 activation and reactivity by bioinorganic active sites.
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