The direct n.m.r. observation of a slowly exchanging, enzyme-bound ligand via photo-CIDNP: a study of the human carbonic anhydrase B–sulphanilamide complex
Abstract
Sulphanilamide, a potent inhibitor of the enzyme carbonic anhydrase, showed a photo-CIDNP 1H n.m.r. spectrum; the resultant polarisation was maintained when the ligand was bound to the enzyme and a new resonance, arising from the slowly exchanging bound species, was observed.