super(13)C and super(15)N NMR and time-resolved fluorescence depolarization study of bovine carbonic anhydrase - 4-methylbenzene-sulfonamide complex

The influence of the binding of the high-affinity inhibitor, 4-methylbenzene-sulfonamide to the active site of bovine carbonic anhydrase B was studied by super(15)N- and super(13)C-NMR spectroscopy. The rotational correlation time dependence on temperature and concentration of the complex was determined by time-resolved fluorescence depolarization measurements. Our experiment provides evidence that the stoichiometry of the interaction of 4-methylbenzene-sulfonamide with carbonic anhydrase B is 1:1 and the inhibitor is bound in anionic form.