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The Root effect.

T Brittain

    Comparative Biochemistry and Physiology. B, Comparative Biochemistry
    |January 1, 1987
    PubMed
    Summary
    This summary is machine-generated.

    The Root effect in hemoglobin, characterized by reduced oxygen binding at low pH, is linked to a specific serine residue. This phenomenon, crucial for oxygenating fish retinas, involves complex molecular interactions.

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    Area of Science:

    • Biochemistry
    • Physiology
    • Molecular Biology

    Background:

    • The Root effect is an exaggerated alkaline Bohr effect observed in certain hemoglobins.
    • It is characterized by a loss of oxygen binding capacity at low pH.
    • This effect is distinct from the normal acid Bohr effect.

    Purpose of the Study:

    • To investigate the molecular basis of the Root effect in hemoglobin.
    • To understand the role of specific amino acid residues, particularly serine at position F9(94) beta.
    • To explore the physiological significance of the Root effect in fish.

    Main Methods:

    • Analysis of hemoglobin structure-function relationships.
    • Comparison of hemoglobins with and without the Root effect.
    • Investigating molecular interactions influencing oxygen affinity.

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    Main Results:

    • A serine residue at position F9(94) beta is critical for the Root effect, though not solely sufficient.
    • Other molecular interactions can negate the stabilizing effect of this serine residue.
    • Loss of cooperativity at low pH is due to stabilization of the low-affinity T state.

    Conclusions:

    • The Root effect is primarily linked to the F9(94) beta serine substitution and other molecular factors.
    • The physiological role is likely related to oxygenating the fish retina, not solely the swim bladder.
    • Heterogeneity within the T state explains observed Hill coefficients below unity.