Jul 1, 1980

Inhibition of cobalt(II) carboxypeptidase A by ligands. Kinetic evidence for the formation of a ternary enzyme-metal-ligand complex

Journal of Inorganic Biochemistry
R J Rogers, E J Billo


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.

  • References3
  • Citations2


  • References3
  • Citations2


Mentioned in this Paper

Carboxypeptidase A
Carboxypeptidase A5
Chelating Agents
Carboxypeptidase A Activity
Plasma Protein Binding Capacity
Metabolic Inhibition

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