A mechanism for indirect allosteric action of charged effectors |
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Authors: | M Brumen S Svetina |
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Institution: | (1) Institute “J. Stefan” and Institute of Biophysics, Medical Faculty, University of Ljubljana, Ljubljana, Yugoslavia |
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Abstract: | A mechanism for indirect allosteric action of charged effectors on substrate binding to a macromolecule is proposed. It is
accounted for by electrostatic interaction among effectors in the solution, away from their receptors. The possibility of
the mechanism proposed is tested in the allosteric action of univalent salt and 2,3-diphosphoglycerate on oxygen binding to
hemoglobin. A model for electrostatic interaction between these two effectors in the solution and for their overall effect
on oxygen binding is introduced. The 2,3-diphosphoglycerate binding constant to deoxygenated hemoglobin as a function of univalent
salt concentration and the median ligand activity as a function of the concentration of univalent salt and 2,3-diphoshoglycerate
are calculated and compared with experimental data. The obtained results indicate that electrostatic interaction in the solution
may significantly contribute to indirect allosteric action of charged effectors.
Partly presented at the “11th FEBS Meeting” in Copenhagen, August 1977 |
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Keywords: | Hemoglobin Oxygen binding Charged allosteric effectors Model |
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