Anion binding to a protein-protein complex lacks dependence on net charge.
The binding of anions to proteins occurs in numerous physiological and metabolic processes. In an effort to understand the factors important in these interactions, we have studied the weak binding of phosphate and sulfate to a protein-protein complex using isothermal titration calorimetry. To our knowledge, this is the first system in which the thermodynamics of anion binding have been determined calorimetrically. By studying both phosphate and sulfate binding and using a range of pH values, the charge on the anion was varied from approximately -1 to -2. Surprisingly, no dependence of the binding energetics on the charge of the anion was observed. This result indicates that charge-charge interactions are not the dominant factor in binding and suggests the importance of hydrogen bonding in specifically recognizing and coordinating anions.
Waldron
Travis T
TT
University of Iowa, Roy J. and Lucille A. Carver College of Medicine, Department of Biochemistry, Iowa City, Iowa 52242, USA.
Modestou
Modestos A
MA
Murphy
Kenneth P
KP
D000818:Animals; D002151:Calorimetry; D004527:Egg Proteins / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D017680:Potassium Compounds / Q000378:metabolism*; D055672:Static Electricity; D013431:Sulfates / Q000378:metabolism*; D013816:Thermodynamics; D014422:Turkeys
D004527:Egg Proteins; D010710:Phosphates; D017680:Potassium Compounds; D013431:Sulfates; C012036:sodium sulfate; C013216:potassium phosphate; C018279:sodium phosphate