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[Current conception of the Bohr effect].

C F Poyart, E Bursaux

Le Poumon Et Le Coeur

|January 1, 1975

Summary

This summary is machine-generated.

The Bohr effect, crucial for oxygen transport, is explained by molecular changes in hemoglobin. Carbon dioxide and diphosphoglycerate influence this effect by binding to hemoglobin, altering oxygen affinity and release.

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Area of Science:

Biochemistry
Molecular Biology
Physiology

Context:

The Bohr effect describes how blood pH and carbon dioxide levels affect oxygen binding to hemoglobin.
Understanding this mechanism is vital for respiratory and circulatory physiology.

Purpose:

To elucidate the molecular underpinnings of the Bohr effect using Perutz's molecular model.
To explain how carbon dioxide and diphosphoglycerate modulate hemoglobin's oxygen affinity and the Bohr effect.

Summary:

The Bohr effect arises from alterations in the pK of globin chain groups during conformational changes between deoxy and oxyhemoglobin.
Carbon dioxide forms carbamino compounds, predominantly on deoxygenated hemoglobin, which reduces both oxygen affinity and the Bohr effect.
Diphosphoglycerate binds to hemoglobin, decreasing oxygen affinity but enhancing the Bohr effect.

Impact:

Provides a molecular explanation for the Bohr effect, integrating the roles of carbon dioxide and diphosphoglycerate.
Highlights the complex interplay of pH, oxygen saturation, carbon dioxide partial pressure, and DPG concentration in regulating the Bohr effect in red blood cells.