Decomposition kinetics of Ni(III)-peptide complexes with histidine and histamine as the third residue

The decomposition kinetics of the Ni(III) complexes of Gly(2)HisGly and Gly(2)Ha are studied from p[H(+)] 3.5 to 10, where His is l-histidine and Ha is histamine. In these redox reactions, at least two Ni(III) complexes are reduced to Ni(II) while oxidizing a single peptide ligand. The rate of Ni(III) loss is first order at low pH, mixed order from pH 7.0 to 8.5, and second order at higher pH. The transition from first- to second-order kinetics is attributed to the formation of an oxo-bridged Ni(III)-peptide dimer. The rates of decay of the Ni(III) complexes are general-base assisted with Brønsted beta values of 0.62 and 0.59 for Ni(III)Gly(2)HisGly and Ni(III)Gly(2)Ha, respectively. The coordination of Gly(2)HisGly and Gly(2)Ha to Ni(II) are examined by UV-vis and CD spectroscopy. The square planar Ni(II)(H(-2)Gly(2)HisGly)(-) and Ni(II)(H(-2)Gly(2)Ha) complexes lose an additional proton from an imidazole nitrogen at high pH with pK(a) values of 11.74 and 11.54, respectively. The corresponding Ni(III) complexes have axially coordinated water molecules with pK(a) values of 9.37 and 9.44. At higher pH an additional proton is lost from the imidazole nitrogen with a pK(a) value of 10.50 to give Ni(III)(H(-3)Gly(2)Ha)(H(2)O)(OH)(2-).