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Carbon monoxide binding to human hemoglobin A0.

E Di Cera1, M L Doyle, P R Connelly

  • 1Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.

Biochemistry
|October 6, 1987
PubMed
Summary
This summary is machine-generated.

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Carbon monoxide and oxygen binding curves to human hemoglobin are not parallel, invalidating Haldane's laws. The partition coefficient varies with saturation, challenging previous models of hemoglobin function.

Area of Science:

  • Biochemistry
  • Physiological Chemistry

Background:

  • Human hemoglobin A0 exhibits complex oxygen and carbon monoxide binding kinetics.
  • Haldane's laws traditionally describe gas partitioning in hemoglobin, but require re-evaluation.
  • Allosteric models provide a framework for understanding hemoglobin's cooperative binding behavior.

Purpose of the Study:

  • To precisely measure the carbon monoxide binding curve of human hemoglobin A0.
  • To compare the carbon monoxide and oxygen binding curves under identical conditions.
  • To test the validity of Haldane's laws and refine understanding of hemoglobin-ligand interactions.

Main Methods:

  • High-precision measurement of carbon monoxide binding to hemoglobin A0.
  • Comparative analysis of oxygen and carbon monoxide binding curves.

Related Experiment Videos

  • Application of the allosteric model to interpret binding data.

    • Main Results:

    • The carbon monoxide and oxygen binding curves for hemoglobin are demonstrably not parallel.
    • Haldane's two laws for gas partitioning to hemoglobin are invalidated by these findings.
    • The partition coefficient between CO and O2 is significantly lower at low saturation than previously reported.
    • The T and R states of hemoglobin exhibit distinct partition coefficients for CO and O2.

    Conclusions:

    • The non-parallel binding curves necessitate a revision of established models for hemoglobin-gas interactions.
    • The allosteric model successfully accounts for the observed binding behavior, including the negligible triply ligated species.
    • Understanding the differential binding properties of CO and O2 is crucial for comprehending hemoglobin's physiological role.