Studies of Zn(II) and Co(II) complexes of imidazole and n-methylimidazole with regard to the activity related ionization in carbonic anhydrase.
Mixed aquo-N-methylimidazole complexes of Co(II) have been studied as a function of pH to gain a fuller understanding of the metal-binding site in Co(II)-carbonic anhydrase. The inherent affinity of N-methylimidazole for Co(II) has been calculated along with a species distribution for the stepwise addition of ligand to the metal ion. From these studies, it is apparent that the occurrence of Zn(II) rather than Co(II) in native carbonic anhydrase can be explained by the stronger affinity of Zn(II) for imidazole and the preference of Zn(II) for a tetrahedral geometry as offered by the enzyme. Octahedral Co(II) fails to ionize metal bound water. However, at high pH, Co(II)-N-methylimidazole complexes interact directly with the hydroxide ion, generating species with visible spectra very similar to that of Co(II)-carbonic anhydrase. Tentative structures have been proposed for these species.
D001665:Binding Sites; D002256:Carbonic Anhydrases / Q000378:metabolism; D003035:Cobalt / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D006878:Hydroxides / Q000378:metabolism; D007093:Imidazoles / Q000494:pharmacology*; D011485:Protein Binding; D013329:Structure-Activity Relationship; D015032:Zinc / Q000494:pharmacology*
D006878:Hydroxides; D007093:Imidazoles; D003035:Cobalt; D002256:Carbonic Anhydrases; D015032:Zinc