Thermodynamics of Binding of d-Galactose and Deoxy Derivatives thereof to the l-Arabinose-binding Protein

We report the thermodynamics of binding of d-galactose and deoxy derivatives thereof to the arabinose binding protein (ABP). The “intrinsic” (solute−solute) free energy of binding ΔG°_int at 308 K for the 1-, 2-, 3-, and 6-hydroxyl groups of galactose is remarkably constant (∼−30 kJ/mol), despite the fact that each hydroxyl group subtends different numbers of hydrogen bonds in the complex. The substantially unfavorable enthalpy of binding (∼30 kJ/mol) of 1-deoxygalactose, 2-deoxygalactose, and 3-deoxygalactose in comparison with galactose, cannot be readily accounted for by differences in solvation, suggesting that solute−solute hydrogen bonds are enthalpically significantly more favorable than solute−solvent hydrogen bonds. In contrast, the substantially higher affinity for 2-deoxygalactose in comparison with either 1-deoxygalactose or 3-deoxygalactose derives from differences in the solvation free energies of the free ligands.