The complexation of Zn(II) with glycyl-L-histidylglycine and its deuterated derivatives, glycyl-d2-L-histidyl-glycine and glycyl-L-histidylglycine-d2, was studied by proton nuclear magnetic resonance spectroscopy over the pD range, from 3.4 to 11.0, at 25°C. Addition of Zn(II) to the peptide made the resonances of both imidazole C2-H and C4-H and both methylene-protons of glycyl residues at the amino-terminal and carboxylate end split to three lines in the pD range above 7.0. From the behavior of the C2-H and C4-H chemical shifts, formation of at least two species, in which the imidazole and amino nitrogens coordinated to the metal ion forming a chelate ring, was suggested. Those two species, the ratio of which varied depending on the total concentrations of complexes, seemed to be interconvertible; one referred to as B is a monomer and the other, referred to as C, may be a dimeric or polymeric complex.