Bohr effect and rightward shifts

Bohr effect and rightward shifts

Bohr effect and rightward shifts

On this page

O2-Hb Dissociation Curve - Shifty Business

O2-Hb Dissociation Curve Shifts & P50

  • Curve: Sigmoid shape, plots $SaO_2$ (Y-axis) vs. $PaO_2$ (X-axis), showing hemoglobin's affinity for oxygen.
  • P50: The $PaO_2$ where hemoglobin is 50% saturated. Normal P50 ≈ 27 mmHg.
  • Rightward Shift: Indicates ↓ O2 affinity, facilitating O2 unloading to tissues. A higher P50 means lower affinity.
  • 📌 CADET, face Right! for factors causing a rightward shift:
    • ↑ $CO_2$
    • ↑ Acid (↓ pH)
    • ↑ 2,3-DPG
    • ↑ Exercise
    • ↑ Temperature

⭐ The curve's sigmoid shape is a result of cooperative binding; as one O2 molecule binds to hemoglobin, the affinity for subsequent O2 molecules increases.

Bohr Effect - Letting Go of O2

Describes how ↑$PCO_2$ and ↑$H^+$ (↓pH) decrease hemoglobin's affinity for oxygen, enhancing $O_2$ release. This rightward shift of the oxygen-hemoglobin curve ensures oxygen delivery to metabolically active tissues.

  • Mechanism: $H^+$ and $CO_2$ are allosteric inhibitors that stabilize the deoxygenated (T-state) of hemoglobin, promoting ↓Hb-$O_2$ affinity.
  • Key Drivers in Tissues:
    • ↑$H^+$ (acidosis)
    • ↑$PCO_2$
  • Chemical Basis: $H_2O + CO_2 \rightleftharpoons H_2CO_3 \rightleftharpoons H^+ + HCO_3^-$
  • 📌 Mnemonic: Think CO₂ and Acid for the "C****ADET, face Right!" shift.

⭐ The Bohr effect is most prominent in the peripheral tissues, where high metabolic activity generates CO2 and acids, signaling a need for oxygen.

Rightward Shift Factors - CADET, face Right!

The oxygen-hemoglobin dissociation curve illustrates hemoglobin's affinity for O₂. A shift to the right indicates decreased affinity, facilitating O₂ release to tissues. A left shift signifies increased affinity, promoting O₂ uptake in the lungs. The P₅₀ is the partial pressure of O₂ at which hemoglobin is 50% saturated.

Right Shift (↓ Affinity)Left Shift (↑ Affinity)
↑ P₅₀↓ P₅₀
↑ CO₂↓ CO₂
↓ pH (↑ Acid)↑ pH (↓ Acid)
↑ 2,3-DPG↓ 2,3-DPG
↑ Temperature↓ Temperature
↑ ExerciseFetal Hemoglobin (HbF)

⭐ Fetal hemoglobin (HbF) has a low affinity for 2,3-DPG, resulting in a left-shifted curve compared to adult hemoglobin (HbA). This higher O₂ affinity facilitates O₂ transfer from the mother to the fetus across the placenta.

Haldane Effect - CO2's Ride Home

  • In tissues, deoxygenated hemoglobin has a higher affinity for $CO_2$ and $H^+$, facilitating $CO_2$ uptake from tissues.
    • Forms carbaminohemoglobin ($Hb-CO_2$).
    • Buffers $H^+$, promoting conversion of $CO_2$ to bicarbonate ($HCO_3^-$) via the chloride shift.
  • In the lungs, the binding of $O_2$ to hemoglobin decreases its affinity for $CO_2$, causing its release into the alveoli for expiration.

⭐ The Haldane effect is quantitatively more important for promoting $CO_2$ transport than the Bohr effect is for promoting $O_2$ transport.

📌 Haldane in the High-O2 Lungs helps release H+ from Hb.

High‑Yield Points - ⚡ Biggest Takeaways

  • The Bohr effect is a rightward shift of the oxygen-hemoglobin curve, driven by ↑ PCO₂ or ↓ pH.
  • This shift decreases hemoglobin's affinity for O₂, promoting oxygen unloading in metabolically active tissues.
  • Key factors causing a rightward shift are ↑ CO₂, ↑ Acid, ↑ 2,3-DPG, ↑ Exercise, and ↑ Temperature.
  • Protons (H⁺) and CO₂ act as allosteric inhibitors, stabilizing the taut (T) form of hemoglobin.

Practice Questions: Bohr effect and rightward shifts

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?

1 of 5

Flashcards: Bohr effect and rightward shifts

1/10

Carboxyhemoglobin causes _____ O2-binding capacity

TAP TO REVEAL ANSWER

Carboxyhemoglobin causes _____ O2-binding capacity

decreased

browseSpaceflip

Enjoying this lesson?

Get full access to all lessons, practice questions, and more.

Start Your Free Trial