PMID: 6163446Feb 3, 1981Paper

Electrostatic effects in hemoglobin: electrostatic energy associated with allosteric transition and effector binding

Biochemistry
J B MatthewF R Gurd

Abstract

The pH dependence of the summed electrostatic stabilization for deoxy- and liganded hemoglobin was computed for several ionic strength values. The computed contribution to the stabilization of deoxyhemoglobin by binding of 2,3-diphosphoglycerate in the beta cleft compared well with experimental binding behavior for human hemoglobin A0 and hemoglobin F. The contribution of diphosphoglycerate binding to the alkaline Bohr effect was computed correctly for both hemoglobins A0 and F. The computed effects of simultaneous binding of diphosphoglycerate and formation of Val-1 beta carbamino adducts suggested a competition between these effectors. A direct competition was formulated between these two effectors, with extension to include a simple anion such as chloride or bicarbonate binding in competition with diphosphoglycerate but not with Val-1 beta carbamino formation. This model was found to hold at pH 7.3-7.4 over a range of concentrations of the effectors involved and to predict the pH dependence of Val-1 beta carbamino formation over the pH range 7.0-8.0. The pH dependence of the computed differential stability of liganded vs. unliganded hemoglobin A compared well with observation.

References

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Citations

Jan 1, 1986·Progress in Biophysics and Molecular Biology·N K Rogers
Nov 9, 1989·Biochimica Et Biophysica Acta·P LundbergE Chiancone
Aug 31, 1990·Biophysical Chemistry·M R Busch, C E Ho
Feb 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·S A HeftaF R Gurd
Jan 1, 1985·CRC Critical Reviews in Biochemistry·J B MatthewS J Shire
Mar 15, 1984·Journal of Molecular Biology·A A Rashin, B Honig
Dec 1, 1984·Biopolymers·J B Matthew, F M Richards
Sep 28, 1982·Biochemistry·J B Matthew, F M Richards

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