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pubmed-article:3139026pubmed:abstractTextBinding of 4-fluorobenzenesulfonamide to human carbonic anhydrases I and II has been studied by proton, fluorine, and nitrogen-15 nuclear magnetic resonance spectroscopy. All three types of experiments provide evidence that the stoichiometry of the interaction of this inhibitor with both enzymes is 2 mol of inhibitor bound per mole of enzyme. Observations which suggest that the bound forms are involved in an exchange process that is rapid at room temperature but slower at 2 degrees C are described. Nitrogen-15 shift data show that the bound inhibitors are present at the active site as anions. The proton experiments indicate appreciable reorganization of the tertiary structure of the protein upon binding. Saturation-transfer experiments to determine the rate of dissociation of the inhibitor-enzyme complex lead to the conclusion that the dissociation process is more complicated than a simple free-bound equilibrium.lld:pubmed
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pubmed-article:3139026pubmed:authorpubmed-author:GerigJ TJTlld:pubmed
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pubmed-article:3139026pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:3139026pubmed:year1988lld:pubmed
pubmed-article:3139026pubmed:articleTitleNMR studies of carbonic anhydrase-4-fluorobenzenesulfonamide complexes.lld:pubmed
pubmed-article:3139026pubmed:affiliationDepartment of Chemistry, University of California, Santa Barbara 93106.lld:pubmed
pubmed-article:3139026pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:3139026pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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