Nitrogen-15 nuclear magnetic resonance study of benzenesulfonamide and cyanate binding to carbonic anhydrase.

@article{Kanamori1983Nitrogen15NM,
  title={Nitrogen-15 nuclear magnetic resonance study of benzenesulfonamide and cyanate binding to carbonic anhydrase.},
  author={K. Kanamori and J. Roberts},
  journal={Biochemistry},
  year={1983},
  volume={22 11},
  pages={
          2658-64
        }
}
The binding of inhibitors, cyanate and benzenesulfonamide, to the active-site zinc of human carbonic anhydrase B was studied by ^(15)N nuclear magnetic resonance spectroscopy. The cyanate nitrogen resonance moved 34 ppm upfield on binding to the enzyme. The shielding is comparable to that reported for a zinc-isocyanate complex and strongly suggests complexation of cyanate to zinc through nitrogen. The proton-coupled ^(15)N resonance of the enzyme-bound benzenesulfonamide was a doublet… Expand
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