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    Area of Science:

    • Biochemistry
    • Evolutionary Biology
    • Marine Biology

    Background:

    • Hemocyanins (Hcs) are copper-containing proteins responsible for oxygen transport in many invertebrates.
    • The evolutionary origins of respiratory pigments in bivalves are not fully understood.
    • Previous hypotheses suggested hemoglobin as the ancestral bivalve oxygen carrier.

    Purpose of the Study:

    • To investigate the properties of the hemocyanin-like molecule in primitive bivalves (protobranchs).
    • To determine the evolutionary history of oxygen carriers in bivalves.

    Main Methods:

    • Analysis of the hemocyanin-like molecule's O2 binding properties.
    • Sedimentation behavior analysis.
    • Comparison of molecular weight and structural characteristics with other molluscan hemocyanins.

    Main Results:

    • The hemocyanin-like molecule in protobranchs reversibly binds O2 and exhibits distinctive respiratory and sedimentation properties.
    • Its molecular weight is consistent with a structure comprising two octopod hemocyanins.
    • Hemocyanin is present in both solemyoids and nuculoids, supporting the Protobranchia taxon.
    • This finding contrasts with the presence of intracellular hemoglobin in less primitive bivalves (Pteriomorpha).

    Conclusions:

    • Hemocyanin is likely the primitive oxygen carrier in bivalves.
    • Hemoglobin evolved independently at least twice in bivalves, replacing hemocyanin in some lineages.