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Kinetics and mechanisms of the recombination of zinc ii cobalt ii and nickel ii with the metal depleted catalytic site of horse liver alcohol dehydrogenase ec 1.1.1.1


Kinetics and mechanisms of the recombination of zinc ii cobalt ii and nickel ii with the metal depleted catalytic site of horse liver alcohol dehydrogenase ec 1.1.1.1



Journal of Inorganic Biochemistry 18(1): 59-70



ISSN/ISBN: 0162-0134

The kinetics of the recombination of the metal-depleted active site of horse liver alcohol dehydrogenase (LADH) with metal ions were studied over a range of pH and temperature. The formation rates were determined optically, by activity measurements, or by using the pH change during metal incorporation with a pH indicator as monitor. The binding of Zn2+, Co2+ and Ni2+ ions occurs in a 2 step process. The 1st step is a fast equilibrium reaction, characterized by an equilibrium constant K1. The spectroscopic and catalytic properties of the native or metal-substituted protein are recovered in a slow, monomolecular process with the rate constant k2. The rate constants k2 are 5.2 .cntdot. 10-2 sec-1 (Zn2+), 1.1 .cntdot. 10-3 sec-1 (Co2+) and 2 .cntdot. 10-4 sec-1 (Ni2+). The rate constants increase with increasing pH. Using temperature dependence, the activation parameters for the reaction with Co2+ and Ni2+ were determined. Activation energies of 51 .+-. 2.5 kJ/mol (0.033 M N-Tris-(hydroxymethyl)methyl-2-aminomethane sulfonic acid (TES), pH 6.9) for Co2+ and 48.5 .+-. 4 kJ/mol (0.033 M TES, pH 7.2) for Ni2+ at 23.degree. C were found. The corresponding activation entropies are -146 .+-. 10 kJ/mol K for Co2+ and -163 .+-. 9 kJ/mol K for Ni2+. Two protons are released during the binding of Zn2+ to H4Zn(n)2 LADH in the pH range 6.8-8.1. The binding of coenzyme, either reduced or oxidized, completely prevents the incorporation of metal ions, suggesting that the metal ions enter the catalytic site via the coenzyme binding domain and not through the hydrophobic substrate channel.

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Related references

Kinetics and mechanisms of the recombination of Zn2+, Co2+, and Ni2+ with the metal-depleted catalytic site of horse liver alcohol dehydrogenase. Journal of Inorganic Biochemistry 18(1): 59-69, 1983

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