Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II

The structural and functional consequences of positively charged, negatively charged, and neutral groups incorporated at the para position of benzenesulfonamide carbonic anhydrase (CA) inhibitors are reported. The results have indicated that positively charged moieties should be avoided in the design of linker segments and such charges are more poorly tolerated by CA I when compared to CA II.