Structural insights into the O2 reduction mechanism of multicopper oxidase
Abstract
Multicopper oxidases are ubiquitous enzymes that catalyse the oxidation of various substrates via the reduction of O2 to H2O. The enzymes contain a common active centre consisting of four copper ions. The key component for O2 reduction is the trinuclear copper centre comprising one type II and a pair of type III copper ions. Although the crystal structures of many multicopper oxidases have been determined by X-ray crystallography, the geometric parameters in the trinuclear copper centre are different for each study. Recent studies have revealed that the redox state of copper ions is altered by X-ray irradiation. The reported crystal structures may represent mixtures of different stages of the catalytic reactions. In this review, we discuss recent findings related to the structure of the active site in multicopper oxidases.
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