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Biochemistry Chemistry of Hemoglobin

Oxygen Dissociation Curve and Bohr Effect

Topic overview

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Hemoglobin’s sigmoidal oxygen dissociation curve arises from transitions between lower-affinity T and higher-affinity R states. P₅₀ marks the oxygen partial pressure at 50% saturation; a higher P₅₀ indicates lower oxygen affinity and a right shift. Increased CO₂, increased H⁺, higher temperature, and increased 2,3-BPG are among the factors associated with a right shift. In the Bohr effect, CO₂ and H⁺ stabilize the T state, encouraging oxygen release in tissues; in the lungs, the reverse conditions support oxygen loading. The lesson also distinguishes the Bohr effect from the Haldane effect and explores how 2,3-BPG, fetal hemoglobin, stored blood, and high altitude influence the curve.

Learning objectives

What you'll learn

  • Explain how positive cooperativity produces hemoglobin’s sigmoidal oxygen dissociation curve.
  • Interpret P₅₀ and relate right and left shifts to oxygen affinity.
  • Describe how CO₂ and H⁺ influence hemoglobin oxygen binding through the Bohr effect.
  • Distinguish the Bohr effect from the Haldane effect.
  • Identify how 2,3-BPG and selected physiological scenarios modify the curve.
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