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J. Biochem, 1977, Vol. 81, No. 5 1383-1391
© 1977 Japanese Biochemical Society

research-article

Coordination Chemical Studies on Metalloenzymes

II. Kinetic Behavior of Various Types of Chelating Agents towards Bovine Carbonic Anhydrase

Yoshinori KIDANI and Junzo HIROSE

Faculty of Pharmaceutical Sciences, Nagoya City University, Tanabe-dori Mizuho-ku, Nagoya, Aichi 467

In order to investigate the kinetics and mechanism of the removal of zinc ions from bovine carbonic anhydrase [EC 4.2.1.1 [EC] ] (BCA), several chelating agents with various stability constants were used to remove zinc from BCA. The second-order rate constants (kapp) of zinc- removal from BCA were found to be in the following order; 2,6-pyridinedicarboxylic acid>>2-pyridinecarboxylic acid> 2,4-pyridinedicarboxylic acid> 2,3-pyridinedicarboxylic acid ≥1,10-phenanthroline≥5-methyl-1,10-phenanthroline>>2,2'-bipyridine. With similar chelating agents. the greater the stability constant, the faster was the rate of removal of zinc ions from BCA. With EDTA, trans-1,2-cyclohexanediaminetetraacetic acid, and nitrilotriacetic acid, the rate of zinc ion removal from the native enzyme was governed by the rate of spontaneous dissociation of the zinc enzyme.

The rate constants for the removal of zinc ions from BCA were governed by the affinity of the chelating agents for the metal ion and the conformation of the chelating agents. Based on these findings, reaction pathways for various chelating agents are proposed.


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