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During turnover, reducing equivalents are derived from substrate and transferred to copper from reduced TPQ. Electrons from dithionite may be transferred to copper via TPQ as well because dithionite can reduce TPQ in most amine oxidases. At this time we cannot rule out the possibility that there may be structural differences between the Cu(I) sites in dithionite-reduced versus substrate-reduced amine oxidases. Owing to the reversible redox partition (Scheme 1 ) the substrate-reduced form is difficult to probe by XAS, especially because the Cu(II) state is favored at low temperatures. The Cu(I) state is stabilized by the addition of cyanide and other exogenous ligands, and structural studies of this complex are underway.
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