Dioxygen galactose oxidase

Copper(II) complexes with phenoxo ligands have attracted great interest, in order to develop basic coordination chemistry for their possible use as models for tyrosinase activity (dimeric complexes) and fungal enzyme galactose oxidase (GO) (monomeric complexes). The latter enzyme catalyzes the two-electron oxidation of primary alcohols with dioxygen to yield aldehyde and... 

Copper would seem to be an appropriate choice of metal for the catalytic oxidation of alcohols with dioxygen since it comprises the catalytic centre in a variety of enzymes, e.g. galactose oxidase, which catalyze this conversion in vivo [188, 189]. Several catalytically active biomimetic models for these enzymes have been designed which are seminal examples in this area [190-193]. A complete overview of this field can be found in a review [194]. 

Borman, C. D., Saysell, C. G., and Sykes, A. G., 1997, Kinetic studies on the reactions of Fusar-ium galactose oxidase with five different substrates in the presence of dioxygen, J. Biol. Inorg. Chem. 2 4809487. 

Galactose Oxidase (GO) from the filamentous wheat-root fungus Fusarium spp. is a mononuclear type 2 copper enzyme that catalyzes the two-electron oxidation of a large number of primary alcohols to their corresponding aldehydes, coupled with the reduction of dioxygen to hydrogen peroxide [1,18] ... 

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