Oxygen-hemoglobin dissociation curve

Oxygen-hemoglobin dissociation curve

Oxygen-hemoglobin dissociation curve

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O₂-Hgb Curve - The S-Shaped Star

Oxygen-hemoglobin dissociation curve

  • Sigmoid (S-shape) curve due to cooperative binding: O₂ binding to one heme group ↑ affinity of others.
  • P₅₀: O₂ partial pressure where hemoglobin is 50% saturated; normally ~26 mmHg.
Right Shift (↓ Affinity)Left Shift (↑ Affinity)
↑ CO₂, ↑ Acid (↓ pH)↓ CO₂, ↓ Acid (↑ pH)
↑ 2,3-DPG, ↑ Temp↓ 2,3-DPG, ↓ Temp
↑ ExerciseFetal Hb (HbF), CO, MetHb

Bohr Effect: In peripheral tissues, ↑ H⁺ and ↑ CO₂ promote O₂ release from hemoglobin, causing a rightward shift of the curve.

Curve Shifts - Righty Tighty, Lefty Loosey

The curve's position reflects hemoglobin's O₂ affinity. A right shift promotes O₂ unloading in tissues (lower affinity), while a left shift enhances O₂ binding in the lungs (higher affinity).

Oxygen-hemoglobin dissociation curve shifts

FeatureRight Shift (↓ Affinity)Left Shift (↑ Affinity)
P₅₀↑ P₅₀↓ P₅₀
Causes↑ CO₂, ↑ Acid/H⁺ (↓pH), ↑ 2,3-DPG, ↑ Temperature, Exercise↓ CO₂, ↓ Acid/H⁺ (↑pH), ↓ 2,3-DPG, ↓ Temperature, Fetal Hemoglobin (HbF), CO, Methemoglobinemia
Mnemonic📌 CADET, face Right!
(CO₂, Acid, 2,3-DPG, Exercise, Temperature)

Clinical Curves - When Hemoglobin Misbehaves

  • Curve Shifts: Changes in hemoglobin's affinity for oxygen ($O_2$).
    • Left Shift: ↑ Affinity (Loves $O_2$). Less $O_2$ delivered to tissues.
    • Right Shift: ↓ Affinity (Releases $O_2$). More $O_2$ delivered to tissues.

Oxygen-hemoglobin dissociation curve with shifts and factors

Left Shift (↑ Affinity)FactorRight Shift (↓ Affinity)
↓ $H^+$ (↑ pH)Acidity↑ $H^+$ (↓ pH)
↓ TempTemp.↑ Temp
↓ 2,3-BPG2,3-BPG↑ 2,3-BPG
↑ COCO
↑ Met-HbMethemoglobin
↑ HbFFetal Hb

⭐ In CO poisoning, $PaO_2$ is normal, but $SaO_2$ is low. CO causes a left shift, trapping $O_2$ on hemoglobin.

  • The sigmoidal shape of the curve is due to cooperative binding.
  • A right shift indicates decreased O₂ affinity, facilitating O₂ unloading to tissues.
  • Factors causing a right shift (CADET): ↑ CO₂, Acid (↓pH), 2,3-DPG, Exercise, Temperature.
  • A left shift signifies increased O₂ affinity, promoting O₂ loading in the lungs.
  • Key causes of a left shift include fetal hemoglobin (HbF) and CO poisoning.
  • P50 is the PO₂ where hemoglobin is 50% saturated; an ↑ P50 reflects a right shift.

Practice Questions: Oxygen-hemoglobin dissociation curve

Test your understanding with these related questions

A 33-year-old woman is brought to the emergency department 30 minutes after being rescued from a fire in her apartment. She reports nausea, headache, and dizziness. Physical examination shows black discoloration of her oral mucosa. Pulse oximetry shows an oxygen saturation of 99% on room air. The substance most likely causing symptoms in this patient primarily produces toxicity by which of the following mechanisms?

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Flashcards: Oxygen-hemoglobin dissociation curve

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Carbon monoxide binds competitively to Hb and with 200-250x _____ affinity than O2

TAP TO REVEAL ANSWER

Carbon monoxide binds competitively to Hb and with 200-250x _____ affinity than O2

greater

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