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Hemoglobin function in the vertebrates: an evolutionary model.

M L Coates

    Journal of Molecular Evolution
    |December 29, 1975
    PubMed
    Summary
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    Vertebrate hemoglobins evolved from a monomer to a tetramer, gaining cooperativity and Bohr effect. Organic phosphate regulation shifted from ATP to DPG, then IP5 in birds.

    Area of Science:

    • Biochemistry
    • Evolutionary Biology
    • Physiology

    Background:

    • Hemoglobin's quaternary structure, cooperativity, Bohr effect, and organic phosphate regulation vary across vertebrates.
    • Understanding hemoglobin evolution provides insights into vertebrate adaptation and physiological diversity.

    Purpose of the Study:

    • To review comparative data on vertebrate hemoglobin function.
    • To deduce a phylogeny of hemoglobin function in vertebrates.
    • To propose evolutionary pathways for hemoglobin structure and regulation.

    Main Methods:

    • Comparative analysis of published data on hemoglobin structure and function.
    • Phylogenetic reconstruction of hemoglobin evolution based on functional traits.
    • Hypothesizing molecular mechanisms (amino acid substitutions) driving evolutionary changes.

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    Main Results:

    • A proposed evolutionary path from monomeric hemoglobin to a deoxy dimer, then to a tetramer.
    • Early tetrameric hemoglobins likely dissociated into dimers upon oxygenation.
    • Gene duplication preceded the origin of tetrameric oxyhemoglobin.
    • Organic phosphate binding sites evolved through few amino acid substitutions.
    • ATP was the initial organic phosphate regulator, later replaced by DPG, and then IP5 in birds.

    Conclusions:

    • Vertebrate hemoglobin function evolved through a series of structural and regulatory adaptations.
    • The evolution of cooperativity, Bohr effect, and organic phosphate regulation were critical for oxygen transport efficiency.
    • The shift in organic phosphate regulators reflects changes in cellular metabolism and oxygen demand.