Recent Advances in One-Electron-Oxidized CuII–Diphenoxide Complexes as Models of Galactose Oxidase: Importance of the Structural Flexibility in the Active Site

The phenoxyl radical plays important roles in biological systems as cofactors in some metalloenzymes, such as galactose oxidase (GO) catalyzing oxidation of primary alcohols to give the corresponding aldehydes. Many metal(II)–phenoxyl radical complexes have hitherto been studied for understanding the detailed properties and reactivities of GO, and thus the nature of GO has gradually become clearer. However, the effects of the subtle geometric and electronic structural changes at the active site of GO, especially the structural change in the catalytic cycle and the effect of the second coordination sphere, have not been fully discussed yet. In this Review, we focus on further details of the model studies of GO and discuss the importance of the structural change at the active site of GO.