Dynamics of ternary complex formation in the reaction of diaquoanthranilato-N, N-diacetatonickelate(II) with 2,2?-bipyridine and 1,10-phenanthroline

Abstract

Dynamics of ternary complex formation in the reaction of diaquoanthranilato-N, N-diacetatonickelate(II) with 2,2′-bipyridine and 1,10-phenanthroline. $\rm Ni(ada)(H_2O)_2^{-}$ $+$ $L\rightleftharpoons Ni(ada)(L)^{-}$ $+$ $2 H_20;$ $- {{d[Ni(ada)^{-}]}\over{dt}}$ $=$ $k_f[Ni(ada)^{-}][L]+k_d\ [Ni(ada)(L)];$ $\ ada^{3-}=$anthranilate-N, N-diacetate; and L=bipy or phen. The kinetics of formation of ternary complexes by diaquoanthranilato-N, N-diacetatonickelate(II). [Ni(ada)(H2O)]− with 2,2′-bipyridine (bipy) and 1,10-phenanthroline (phen) have been studied under pseudo-first-order conditions containing excess bipy or phen by stopped-flow spectrophotometry in the pH range 7.1–7.8 at 25°C and λ = 0.1 mol dm−3. In each case, the reaction is first-order with respect to both Ni(ada)− and the entering ligand (ie., bipy, phen). The reactions are reversible. The forward rate constants are: $k^{\rm Ni(ada)}_{\rm Ni(ada)(bipy)}=0.87\times10^3{\rm dm}^3 {\rm mol}^{-1}{\rm s}^{-1}$,. $k^{\rm Ni(ada)}_{\rm Ni(ada)(phen)}=1.87\times10^3{\rm dm}^3 {\rm mol}^{-1}{\rm s}^{-1}$; and the reverse rate constants are: $k^{\rm Ni(ada)(bipy)}_{\rm Ni(ada)}=1.0{\rm s}^{-1}$ and $k^{\rm Ni(ada)(phen)}_{\rm Ni(ada)}=2.0{\rm s}^{-1}$. The corresponding stability constants of ternary complex formation are: and , . The observed rate constants and huge drops in stability constants in ternary complex formation agree well with the mechanism in which dissociation of an acetate arm of the coordinated ada3− prior to chelation by the aromatic ligand occurs. The observations have been compared with the kinetics of ternary complex formation in the reaction Ni(ada)− - glycine in which the kinetics involves a singly bonded intermediate, N(ada)((SINGLE BOND)O(SINGLE BOND)N)2− in rapid equilibrium with the reactants followed by a sluggish ring closure step. The reaction with the aromatic ligands conforms to a steady-state mechanism, while for glycine it gets shifted to an equilibrium mechanism. The cause of this difference in mechanistic pathways has been explained. © 1996 John Wiley & Sons, Inc.