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Is there a Root effect in Xenopus hemoglobin?

M Brunori, A Bellelli, B Giardina

    FEBS Letters
    |August 31, 1987
    PubMed
    Summary
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    Xenopus hemoglobin exhibits a Root effect, a pronounced Bohr effect, where oxygen binding is modulated by pH and organic phosphates. This study confirms the stabilization of its T-quaternary state.

    Area of Science:

    • Biochemistry
    • Physiology
    • Comparative Biology

    Background:

    • Hemoglobin's oxygen affinity is regulated by pH and organic phosphates.
    • The Root effect is an extreme manifestation of the Bohr effect, impacting oxygen release.
    • Xenopus hemoglobin's quaternary structure and its modulation require further investigation.

    Purpose of the Study:

    • To reinvestigate the reaction of Xenopus hemoglobin with oxygen and carbon monoxide.
    • To determine if protons and polyphosphates stabilize the T-quaternary state of Xenopus hemoglobin.
    • To elucidate the molecular and structural basis of the Root effect in Xenopus hemoglobin.

    Main Methods:

    • Spectrophotometric analysis of hemoglobin-ligand interactions.
    • Equilibrium and kinetic measurements of oxygen and carbon monoxide binding.

    Related Experiment Videos

  • pH-dependent studies in the presence and absence of organic phosphates (2,3-diphosphoglycerate, inositol hexakisphosphate).

    • Main Results:

    • Xenopus hemoglobin exhibits a significant Root effect across the pH range of 8.5-6.0.
    • Organic phosphates (2,3-diphosphoglycerate, inositol hexakisphosphate) and protons influence hemoglobin's T-quaternary state stabilization.
    • Equilibrium and kinetic data confirm the presence and characteristics of the Root effect.

    Conclusions:

    • Xenopus hemoglobin displays a pronounced Root effect, indicating an extreme Bohr effect.
    • Protons and polyphosphates play a role in stabilizing the T-quaternary structure, influencing oxygen affinity.
    • This study contributes to the molecular and structural understanding of the Root effect in hemoglobin.