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Structural changes at the heme induced by freezing hemoglobin

M R Ondrias, D L Rousseau, S R Simon

    Science (New York, N.Y.)
    |August 7, 1981
    PubMed
    Summary
    This summary is machine-generated.

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    Freezing deoxyhemoglobin dramatically alters iron-histidine bond vibrations, diminishing structural differences. These changes highlight the bond's role in cooperative ligand binding energetics.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Biochemistry

    Background:

    • Deoxyhemoglobin exhibits quaternary structure-dependent vibrational properties.
    • The iron-histidine bond is crucial for ligand binding and cooperative effects in hemoglobin.

    Purpose of the Study:

    • To investigate the impact of freezing on the vibrational properties of the iron-histidine bond in deoxyhemoglobin.
    • To understand the role of protein dynamics and water interactions in the iron-histidine bond's response to temperature changes.

    Main Methods:

    • Resonance Raman scattering measurements were performed on deoxyhemoglobin at various temperatures, including below freezing.
    • Vibrational modes of the iron-histidine bond were analyzed for changes in shape, frequency, and intensity.

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    Main Results:

    • Freezing significantly diminished the quaternary structure-dependent differences in the iron-histidine mode's shape and frequency.
    • Scattering intensity of the iron-histidine mode increased substantially upon freezing.
    • Further cooling to 10 K resulted in a narrower line and a higher frequency shift.

    Conclusions:

    • Dynamical processes and protein-water interactions contribute to the iron-histidine bond's quaternary structure dependence.
    • These findings provide insights into the role of the iron-histidine bond in the energetics of cooperative ligand binding in hemoglobin.