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Biophys J, September 2000, p. 1637-1654, Vol. 79, No. 3

Salt Effects on Ionization Equilibria of Histidines in Myoglobin

Yung-Hsiang Kao,* Carolyn A. Fitch,dagger Shibani Bhattacharya,* Christopher J. Sarkisian,* Juliette T. J. Lecomte,* and Bertrand García-Moreno E.dagger

 *Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802, and  dagger Department of Biophysics, The Johns Hopkins University, Baltimore, Maryland 21218 USA

The salt dependence of histidine pKa values in sperm whale and horse myoglobin and in histidine-containing peptides was measured by 1H-NMR spectroscopy. Structure-based pKa calculations were performed with continuum methods to test their ability to capture the effects of solution conditions on pKa values. The measured pKa of most histidines, whether in the protein or in model compounds, increased by 0.3 pH units or more between 0.02 M and 1.5 M NaCl. In myoglobin two histidines (His48 and His36) exhibited a shallower dependence than the average, and one (His113) showed a steeper dependence. The 1H-NMR data suggested that the salt dependence of histidine pKa values in the protein was determined primarily by the preferential stabilization of the charged form of histidine with increasing salt concentrations rather than by screening of electrostatic interactions. The magnitude and salt dependence of interactions between ionizable groups were exaggerated in pKa calculations with the finite-difference Poisson-Boltzmann method applied to a static structure, even when the protein interior was treated with arbitrarily high dielectric constants. Improvements in continuum methods for calculating salt effects on pKa values will require explicit consideration of the salt dependence of model compound pKa values used for reference in the calculations.

Biophys J, September 2000, p. 1637-1654, Vol. 79, No. 3
© 2000 by the Biophysical Society   0006-3495/00/09/1637/18  $2.00


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