Tritium NMR studies of the human carbonic anhydrase I-benzenesulfonamide complex.
Tritium NMR spectroscopy has been used to examine the complex formed by [4-3H]benzenesulfon-amide and human carbonic anhydrase I. The results show that in solution the inhibitor forms a 1:1 complex with the enzyme. A 100-spin computational model of the system, constructed with reference to crystallographic results, was used to interpret tritium relaxation behavior and 3H{1H} NOEs. The analysis shows that the rate of dissociation of the enzyme-sulfonamide complex is 0.35 s-1 and that the aromatic ring of the inhibitor undergoes rapid rotation while complexed.
Culf
A S
AS
Department of Chemistry, University of California, Santa Barbara 93106, USA.
Gerig
J T
JT
Williams
P G
PG
D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry*; D002256:Carbonic Anhydrases / Q000737:chemistry*; D006801:Humans; D008667:Metalloproteins / Q000737:chemistry; D008956:Models, Chemical; D008968:Molecular Conformation; D019906:Nuclear Magnetic Resonance, Biomolecular; D013449:Sulfonamides / Q000737:chemistry*; D014316:Tritium; D015032:Zinc; D000096926:Benzenesulfonamides
D002257:Carbonic Anhydrase Inhibitors; D002256:Carbonic Anhydrases; D008667:Metalloproteins; D013449:Sulfonamides; D014316:Tritium; D015032:Zinc; D000096926:Benzenesulfonamides