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Related Experiment Videos

Heme proteins: quantum yield determined by the pulse method.

M Brunori, G M Giacometti, E Antonini

    Proceedings of the National Academy of Sciences of the United States of America
    |November 1, 1973
    PubMed
    Summary

    The pulse method accurately measures photodissociation quantum yields in heme proteins. No direct link was found between quantum yield and ligand affinity, and photodissociation is independent of hemoglobin saturation.

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    Area of Science:

    • Biochemistry
    • Photochemistry
    • Spectroscopy

    Background:

    • Heme proteins like myoglobin and hemoglobin are crucial for oxygen transport and cellular respiration.
    • Understanding ligand photodissociation is key to elucidating their function and reaction mechanisms.

    Purpose of the Study:

    • To apply the "pulse method" for accurate and rapid determination of photodissociation quantum yields.
    • To investigate the relationship between quantum yield and ground-state affinity for various ligands in sperm-whale myoglobin and trout hemoglobin I.
    • To explore the dependence of carbon monoxide photodissociation quantum yield on the saturation level in trout hemoglobin I.

    Main Methods:

    • Utilized the "pulse method" for precise measurement of photodissociation quantum yields.
    • Studied photodissociation of carbon monoxide (CO), oxygen (O2), and isocyanides.

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  • Investigated sperm-whale myoglobin and trout hemoglobin I.
  • Extended measurements to varying degrees of saturation for trout hemoglobin I.

    • Main Results:

    • Confirmed that no simple relationship exists between quantum yield and ground-state affinity for the studied ligands and proteins.
    • Demonstrated that the quantum yield of CO photodissociation in trout hemoglobin I is independent of the fractional saturation level.
    • Provided new insights beyond those from the "steady-state" method.

    Conclusions:

    • The "pulse method" is a reliable technique for studying ligand photodissociation in heme proteins.
    • Ligand photodissociation quantum yield is not directly correlated with ligand binding affinity.
    • Photochemical properties of heme proteins, specifically CO photodissociation, are not influenced by the overall saturation of the protein.