Kinetics and mechanism of dissociation of zinc ion from carbonic anhydrase.
The kinetics of dissociation of Zn2+ from the metalloenzyme carbonic anhydrase was measured over a range of pH, temperature, and acetate concentration. The rate of dissociation is extremely slow at neutral pH (t1/2 approximately 3) years, 4 degrees C), but increases in almost direct proportion to the hydrogen ion concentration and is enhanced in the presence of 1,10-phenanthroline or acetate. The thermodynamic stability of the zinc-apoenzyme complex was determined over a range of pH from rate data on binding and dissociation (stability constants 10(9)-10(11) M-1, 25 degrees C). The great stability of the complex and slow exchange of the apoenzyme ligand is attributed, at least in part, to the rigidity of the multidentate protein ligand.
D001051:Apoenzymes / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008954:Models, Biological; D010618:Phenanthrolines / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D013696:Temperature; D015032:Zinc / Q000378:metabolism*
D001051:Apoenzymes; D010618:Phenanthrolines; D002256:Carbonic Anhydrases; D015032:Zinc