Interaction of cobalt-bovine carbonic anhydrase with the acetate ion.
The visible spectra of solutions of cobalt(II) bovine carbonic anhydrase (carbonate hydro-lyase, EC 4.2.1.1) with increasing amounts of acetate have allowed the determination of the apparent inhibition constants and of the extrapolated limit spectra of the completely bound enzyme. The electronic spectra have been interpreted on the basis of the presence of five coordinate adduct species. 13C and 1H NMR spectra have also been recorded and discussed on the basis of the metal enzyme-acetate type of interactions. Titrations by means of NMR spectroscopy of the acetate-cobalt(II) bovine carbonic anhydrase with p-toluenesulfonamide and azide indicate the existence of two binding sites for the acetate group.
D000085:Acetates / Q000494:pharmacology; D000818:Animals; D002256:Carbonic Anhydrases / Q000378:metabolism; D002417:Cattle; D003035:Cobalt / Q000494:pharmacology; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D000085:Acetates; D003035:Cobalt; D002256:Carbonic Anhydrases