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Axial ligand effects on myoglobin stability.

G McLendon, K Sandberg

    The Journal of Biological Chemistry
    |June 10, 1978
    PubMed
    Summary

    Ligand binding significantly stabilizes hemoprotein conformation, with low-spin complexes showing greater stability than high-spin analogs. Metal spin state, not ligand shape, primarily influences myoglobin

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    Area of Science:

    • Biochemistry
    • Physical Chemistry
    • Protein Dynamics

    Background:

    • Hemoproteins, like myoglobin, undergo conformational changes upon ligand binding.
    • Understanding these changes is crucial for elucidating protein function and stability.
    • Quantitative measurement of these effects has been challenging.

    Purpose of the Study:

    • To quantitatively estimate ligand-induced changes in hemoprotein conformational free energy.
    • To assess the impact of metal spin state versus ligand stereochemistry on protein stability.
    • To validate denaturation titration as a method for measuring ligand-induced stabilization.

    Main Methods:

    • Utilized reversible guanidine hydrochloride denaturation.
    • Employed denaturation titration to analyze hemoprotein stability.
    • Analyzed cyanometmyoglobin (MbCN), azido metmyoglobin (MbN3), aquometmyoglobin (MbH2O), and fluorometmyoglobin (MbF).
    • Accounted for spin state equilibria in denaturation complexity.

    Main Results:

    • Low-spin complexes (MbCN, MbN3) are more stable (1.0 +/- 0.1 kcal/mol) than high-spin analogs (MbH2O, MbF).
    • This stability increment is independent of the data analysis model.
    • Corrected analysis shows MbCN and MbN3 possess similar stability, despite steric differences.
    • Metal spin state is a more significant determinant of conformational free energy than ligand stereochemistry.

    Conclusions:

    • Denaturation titration is a valuable method for quantifying ligand-induced stabilization of hemoprotein conformation.
    • The spin state of the metal center plays a dominant role in determining the conformational free energy of myoglobin.
    • Ligand stereochemistry has a lesser impact on conformational stability compared to the metal spin state.

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