Abstract
The equilibria and kinetics of Ni(II) interactions with the two pyridine coenzymes NAD and NADP were investigated by the temperature-jump relaxation technique. Three relaxation times for each system were detected, of which the two slower were characterized in detail as a function of metal ion and ligand concentrations and pH. Results were found to be consistent with a mechanism involving sequential formation of several different 1:1 metal ion complexes, including those in which the various ring systems participated with phosphate bonding. For NADP, a parallel series of steps involving the phosphate-protonated coenzyme was also present. Rate constants were compared to those for corresponding steps in simpler nucleotide and phosphate systems
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