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Conformational equilibria in spin-labeled hemoglobin.

W J Deal, S G Mohlman, M L Sprang

    Science (New York, N.Y.)
    |March 19, 1971
    PubMed
    Summary
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    Spin labeling reveals that deoxyhemoglobin and oxyhemoglobin conformational states are present in each other, indicating sensitivity to carboxy-terminal histidine equilibrium shifts during oxygenation.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Spectroscopy

    Background:

    • Hemoglobin's quaternary structure changes significantly upon oxygenation.
    • Understanding these conformational changes is crucial for elucidating hemoglobin's physiological function.
    • Paramagnetic resonance spectroscopy offers a sensitive probe for molecular dynamics.

    Purpose of the Study:

    • To investigate the conformational equilibrium of hemoglobin using spin-labeling techniques.
    • To determine if deoxyhemoglobin and oxyhemoglobin conformational states coexist under physiological conditions.
    • To correlate spectral changes with the conformational state of carboxy-terminal histidines.

    Main Methods:

    • Spin labeling of hemoglobin.
    • Paramagnetic resonance spectroscopy (EPR).

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  • Analysis of spectral components under varying pH and ionic strength.

    • Main Results:

    • A spectral component characteristic of deoxyhemoglobin was observed in spin-labeled oxyhemoglobin, and vice versa.
    • These spectral features were dependent on pH and ionic strength.
    • The observed spectral changes indicate sensitivity to the conformational equilibrium of carboxy-terminal histidines.

    Conclusions:

    • Hemoglobin exists as an equilibrium mixture of deoxy and oxy conformational states.
    • Oxygenation induces shifts in this equilibrium, primarily affecting carboxy-terminal histidines.
    • Paramagnetic resonance spectroscopy is a valuable tool for studying hemoglobin conformational dynamics.