Model Systems of Catechol Oxidase Historic Overview

Model Systems of Catechol Oxidase Historic Overview 

The interest in catechol oxidase, as well as in other copper proteins with the type 3 active site, is to a large extent due to their ability to process dioxygen from air at ambient conditions. While hemocyanin is an oxygen carrier in the hemolymph of some arthropods and mollusks, catechol oxidase and tyrosinase utilize it to perform the selective oxidation of organic substrates, for example, phenols and catechols. Therefore, establishment of structure-activity relationships for these enzymes and a complete elucidation of the mechanisms of enzymatic conversions through the development of synthetic models are expected to contribute greatly to the design of oxidation catalysts for potential industrial applications. 

The hypothesis of Lintvedt and Thuruya about the formation of the dicopper-catecholate intermediate in the catalytic process [25] was soon after confirmed by 

Another fascinating topic which attracted the attention of many researchers is the difference in the enzymatic activities between catechol oxidase and the structurally related enzyme tyrosinase. Although both enzymes contain type 3 active 

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Model Systems of Catechol Oxidase Historic Overview 109... 

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