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Decrease in oxygen affinity of myoglobin by formylation of vinyl groups of heme.

M Sono, T Asakura

    The Journal of Biological Chemistry
    |July 10, 1975
    PubMed
    Summary
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    Synthetic myoglobins with different heme modifications show altered oxygen binding and optical properties. Formyl groups on the heme significantly impact oxygen affinity and spectral characteristics, indicating protein-heme interactions are crucial.

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Spectroscopy

    Background:

    • Myoglobin's function relies on its heme prosthetic group for oxygen binding.
    • Modifications to the heme structure can alter myoglobin's biochemical and biophysical properties.
    • Understanding these modifications is key to designing artificial oxygen carriers or studying oxygen transport mechanisms.

    Purpose of the Study:

    • To synthesize and characterize novel green synthetic myoglobins.
    • To investigate the impact of specific heme modifications (spirographis, isospirographis, 2,4-diformyl) on myoglobin's optical and oxygen-binding properties.
    • To elucidate the role of protein-heme interactions in modulating these properties.

    Main Methods:

    • Recombinant preparation of synthetic myoglobins by combining horse heart apomyoglobin with modified hemin compounds.

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  • Spectrophotometric analysis to determine absorption maxima (alpha, beta, Soret bands).
  • Oxygen binding affinity measurements (P50) at controlled temperatures.

    • Main Results:

    • Synthetic myoglobins exhibited distinct optical properties and oxygen affinities.
    • Spirographis and 2,4-diformyl myoglobins showed significantly lower oxygen affinities (higher P50) compared to native myoglobin, attributed to electron-withdrawing formyl groups.
    • Isospirographis myoglobin displayed oxygen affinity similar to native myoglobin, suggesting subtle structural influences.

    Conclusions:

    • The presence of electron-attractive formyl side chains on the heme directly influences oxygen affinity and causes optical red shifts.
    • Differences in properties after recombination highlight the significant role of apomyoglobin interactions in modulating heme function.
    • The study suggests that pi bonding plays a role in determining the oxygen-iron bond strength within myoglobin.