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Galactose oxidase reactivity mechanisms

Since both alcoholic oxidation and O2 reduction are two-electron processes, the catalytic reaction is conceptually equivalent to a transfer of the elements of dihydrogen between the two substrates. Biological hydrogen transfer generally involves specialized organic redox factors (e.g., flavins, nicotinamide, quinones), with well-characterized reaction mechanisms. Galactose oxidase does not contain any of these conventional redox factors and instead utilizes a very different type of active site, a free radical-coupled copper complex, to perform this chemistry. The new type of active site structure implies that the reaction follows a novel biochemical redox mechanisms based on free radicals and the two-electron reactivity of the metalloradical complex. [Pg.505]


See other pages where Galactose oxidase reactivity mechanisms is mentioned: [Pg.38]    [Pg.44]    [Pg.5503]    [Pg.5793]    [Pg.51]    [Pg.5502]    [Pg.5792]    [Pg.140]    [Pg.272]   
See also in sourсe #XX -- [ Pg.198 , Pg.199 , Pg.200 , Pg.201 ]




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