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Sequence of oxygen binding by hemoglobin.

T Asakura, P W Lau

    Proceedings of the National Academy of Sciences of the United States of America
    |November 1, 1978
    PubMed
    Summary
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    Spin labels attached to hemoglobin show that oxygen binds equally to alpha and beta chains without organic phosphate. With organic phosphate, oxygen preferentially binds to alpha chains, altering EPR signals before optical changes.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Molecular Biology

    Background:

    • Hemoglobin's oxygen binding is crucial for O2 transport.
    • Understanding subunit-specific oxygenation is key to hemoglobin function.
    • Organic phosphates allosterically modulate hemoglobin's O2 affinity.

    Purpose of the Study:

    • To investigate subunit-specific oxygen binding in hemoglobin.
    • To determine the role of organic phosphates in hemoglobin oxygenation.
    • To utilize spin-labeling electron paramagnetic resonance (EPR) to probe hemoglobin dynamics.

    Main Methods:

    • Attaching nitroxide spin labels to heme propionic acid groups on alpha and beta chains of hemoglobin.
    • Monitoring changes in EPR spectra of spin labels during deoxygenation.

    Related Experiment Videos

  • Measuring absorption spectra to determine oxygen saturation.
  • Analyzing EPR signal changes versus oxygen saturation, with and without organic phosphates (2,3-diphosphoglycerate, inositol hexaphosphate).

    • Main Results:

    • Spin-labeling did not alter hemoglobin's optical or functional properties.
    • EPR signal changes in alpha-heme-spin-labeled hemoglobin correlated proportionally with oxygen saturation, indicating no inherent binding preference.
    • Deviations from a diagonal line in EPR vs. oxygen saturation plots occurred with organic phosphates, showing EPR changes preceded optical changes.
    • Beta-heme-spin-labeled hemoglobin showed opposite deviations, explained by intersubunit interactions.
    • Organic phosphates induce preferential oxygen binding to alpha chains.

    Conclusions:

    • Oxygen binds to alpha and beta chains with equal probability in the absence of organic phosphate.
    • In the presence of organic phosphate, oxygen exhibits preferential binding to the alpha chains of hemoglobin.
    • EPR spin-labeling is a sensitive method to detect functional changes and subunit interactions in hemoglobin.