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Tritium NMR studies of the human carbonic anhydrase I–benzenesulfonamide complex

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Abstract

Tritium NMR spectroscopy has been used to examine the complexformed by [4-3H]benzenesulfon-amide and human carbonicanhydrase I. The results show that in solution the inhibitor forms a 1:1complex with the enzyme. A 100-spin computational model of the system,constructed with reference to crystallographic results, was used tointerpret tritium relaxation behavior and 3H{1H}NOEs. The analysis shows that the rate of dissociation of theenzyme–sulfonamide complex is 0.35 s−1 and thatthe aromatic ring of the inhibitor undergoes rapid rotation while complexed.

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Authors and Affiliations

  1. Department of Chemistry, University of California, Santa Barbara, CA, 93106, U.S.A

    A.S. Culf & J.T. Gerig

  2. The National Tritium Labelling Facility and Structural Biology Division, E.O. Lawrence Berkeley National Laboratory, One Cyclotron Road, Berkeley, CA, 94720, U.S.A

    P.G. Williams

Authors
  1. A.S. Culf
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  2. J.T. Gerig
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  3. P.G. Williams
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Culf, A., Gerig, J. & Williams, P. Tritium NMR studies of the human carbonic anhydrase I–benzenesulfonamide complex. J Biomol NMR 10, 293–299 (1997). https://doi.org/10.1023/A:1018358101811

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