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Oxygen transport in invertebrates.

C P Mangum

    The American Journal of Physiology
    |May 1, 1985
    PubMed
    Summary
    This summary is machine-generated.

    Early oxygen transport likely involved intracellular hemoglobin within red blood cells. Evolution shifted to extracellular proteins, reducing oxygen storage importance and favoring transport, with hemocyanins emerging separately.

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    Area of Science:

    • Evolutionary Biology
    • Biochemistry
    • Physiology

    Background:

    • Oxygen (O2) carrying proteins evolved to facilitate gas exchange and storage.
    • Early O2 transport systems involved intracellular hemoglobin within nucleated red blood cells.
    • The evolution of closed circulatory systems led to the abandonment of red blood cells in favor of extracellular proteins.

    Purpose of the Study:

    • To trace the evolutionary history of oxygen carrying proteins.
    • To understand the functional shifts in O2 transport and storage mechanisms.
    • To compare the roles of hemoglobins, hemerythrins, and hemocyanins in aerobic metabolism.

    Main Methods:

    • Phylogenetic analysis of O2 carrying proteins.
    • Comparative biochemistry of hemoglobin, hemerythrin, and hemocyanin.

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  • Functional assessment of O2 binding and transport capabilities.

    • Main Results:

    • The earliest O2 transport system likely utilized hemoglobin within nucleated red blood cells for storage and transport.
    • Evolution favored extracellular heme proteins with a reduced emphasis on O2 storage.
    • Hemerythrins evolved alongside intracellular hemoglobins, while hemocyanins arose independently with specialized O2 transport functions.

    Conclusions:

    • The prevalence of hemoglobin in vertebrates may be an evolutionary contingency.
    • Hemocyanins, though arising independently, exhibit adaptive O2 binding and significantly contribute to aerobic metabolism.
    • The evolutionary trajectory of O2 carriers highlights a shift from storage to efficient transport for aerobic life.