Polarography of Some Cu(I) Amino Acid Complexes

Abstract
The polarography of copper(I) with some typical amino acids is characterized by disproportionation at the mercury surface typical of uncomplexed copper(I). Methionine complexes are somewhat unique. Apparently copper(II) and copper(I) are bound by different ligand groups. Implications of these findings on the mechanism of the participation of copper in biological electron transfer reactions are discussed.

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