Abstract: | Saturation kinetics are observed in the inhibition of cobalt carboxypeptidase A by the chelating agent 1,10-phenanthroline. The association constant K1 for the formation of the enzyme-metal-ligand ternary complex and k2, the rate of breakup of the ternary complex, have been obtained. A mechanism is proposed to account for the pH profile of the reaction which, in conjunction with K1, permits the calculation of the individual rate constants k1, K?1, k2, k3. The magnitude of the rate constant k1 suggests that cobalt(II) in CoCPA is five-coordinate. Similar but less extensive studies on inhibition by 2,2′-bipyridyl and 8-hydroquinoline-5-sulfonic acid have also been carried out |