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Hydration and allosteric transitions in hemoglobin

A Bellelli1, A Brancaccio, M Brunori

  • 1Department of Biochemical Sciences, University of Rome La Sapienza, Italy.

The Journal of Biological Chemistry
|March 5, 1993
PubMed
Summary
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Neutral solutes like sucrose decrease human hemoglobin oxygen affinity by stabilizing its T-state. However, this study finds sucrose does not affect trout hemoglobin or human hemoglobin dissociation, challenging previous explanations.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Biophysics

Background:

  • Neutral solutes, such as sucrose, are known to reduce the oxygen affinity of human hemoglobin.
  • This phenomenon was previously attributed to the stabilization of the deoxy-T quaternary state of hemoglobin A, mediated by a decrease in the water activity coefficient.
  • Crystallographic data supported this by showing increased surface area burial at the alpha 1 beta 2 interface in the deoxy-T state compared to the oxy-R state.

Purpose of the Study:

  • To investigate the effect of sucrose on the oxygen affinity of trout hemoglobin I, a cooperative but non-allosteric hemoglobin.
  • To examine the influence of sucrose on the dissociation of human hemoglobin A-CO into dimers, particularly in the presence and absence of inositol hexakisphosphate (IHP).
  • To re-evaluate the prevailing hypothesis regarding the mechanism of neutral solute effects on hemoglobin quaternary structure stabilization.

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Main Methods:

  • Measurement of oxygen binding affinity for trout hemoglobin I in the presence of sucrose.
  • Analysis of human hemoglobin A-CO dissociation into dimers under varying sucrose concentrations and in the presence of IHP.
  • Comparison of experimental findings with existing crystallographic and thermodynamic models.

Main Results:

  • Sucrose demonstrated no effect on the oxygen affinity of trout hemoglobin I, despite its cooperative oxygen binding.
  • Sucrose either increased the dissociation of human hemoglobin A-CO into dimers or had no effect (when IHP was present).
  • These findings contrast with the proposed mechanism involving stabilization of the T-state through water activity reduction.

Conclusions:

  • The observed lack of effect of sucrose on trout hemoglobin and its influence on human hemoglobin dissociation suggest that the mechanism proposed by Colombo et al. may not be universally applicable.
  • The results necessitate a reconsideration of the hypothesis that neutral solutes stabilize the deoxy-T quaternary state of hemoglobin A by reducing water activity.
  • Further research is needed to elucidate the precise molecular interactions governing the effects of neutral solutes on hemoglobin function and quaternary structure.