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Hydroxide ion catalysis of the mono- and bis(triglycinato)cuprate(II) interconversion and the preference for cis vs. trans N-peptide bonding to copper(II).

The Cu(H-2GGG)- complex (where GGG - is the triglycinate ion and the protons are ionized from two peptide nitrogens coordinated to copper(II)) reacts with excess GGG - to form Cu(HL1GGG)22-: Cu(H_2GGG)- + GGG - + OH - <=* Cu(H-iGGG)22~ + OH - (ki, Ic1). The formation and dissociation rates are catalyzed by hydroxide ion, and the values of the rate constants (25.0°, 0.10 /u) are kt = (1.26 ± 0.02) X 10 7 M -2 sec-1 and kT = (8.8 ± 0.3) X 10 4 M -1 sec-1. In the proposed reaction mechanism the hydroxide ion deprotonates an in­ coming peptide group of one triglycine as the Cu-N(peptide) bond of another triglycine breaks. A combination of absorption and circular dichroism spectrophotometry, kinetic results, and model studies indicate that Cu(H_y- GGG)22- exists in a planar form in which the two triglycine molecules are arranged around the copper in a cis bidentate configuration. Infrared and Raman results show that the doubly deprotonated bis complex of glycin- amide with copper(II) also adopts a cis geometry. It is postulated that strong a donation from the deprotonated peptide-nitrogen to copper(II) causes a preference for the cis rather than the trans configuration.