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Myoglobin interspecies structural differences: effects on autoxidation and oxygenation.

D J Livingston, D A Watts, W D Brown

    Archives of Biochemistry and Biophysics
    |August 15, 1986
    PubMed
    Summary
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    Yellowfin tuna myoglobin shows faster oxygen release and higher autoxidation rates compared to sea turtle and sperm whale myoglobin. Autoxidation appears more influenced by ligand access than protein stability.

    Area of Science:

    • Biochemistry
    • Comparative Physiology
    • Protein Chemistry

    Background:

    • Myoglobin (Mb) is crucial for oxygen storage and transport in vertebrates.
    • Variations in Mb structure can affect its oxygen-binding and stability properties.
    • Understanding these variations provides insights into protein function and evolution.

    Purpose of the Study:

    • To compare the thermodynamic and kinetic parameters of oxygenation and autoxidation in myoglobins from yellowfin tuna, Pacific green sea turtle, and sperm whale.
    • To investigate the relationship between protein structure, dynamic stability, and autoxidation susceptibility.

    Main Methods:

    • Oxygen equilibrium measurements were conducted across a temperature range of 10-40°C.
    • Kinetic parameters for oxygenation and autoxidation were determined.

    Related Experiment Videos

  • The influence of ionic strength on autoxidation rates was analyzed.

    • Main Results:

    • Pacific green sea turtle myoglobin exhibited lower oxygen affinity, enthalpy, and entropy for oxygen binding.
    • Yellowfin tuna myoglobin demonstrated the fastest oxygen dissociation rate and highest autoxidation susceptibility.
    • Autoxidation rate dependence on ionic strength was consistent across all three myoglobins, irrespective of dynamic stability differences.

    Conclusions:

    • Ligand accessibility, rather than dynamic protein stability, is a key determinant of myoglobin autoxidation rates.
    • Structural differences in non-heme contact residues significantly impact myoglobin's functional properties.
    • Comparative studies of myoglobin from diverse species reveal important structure-function relationships.