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Home/Biophysics, Fluids & Geoscience/Oxygen-Hemoglobin Dissociation Curve

Oxygen-Hemoglobin Dissociation Curve

This simulator plots the oxygen-hemoglobin dissociation curve using the Hill equation S = pO₂ⁿ/(P50ⁿ+pO₂ⁿ), where S is fractional hemoglobin saturation, n controls cooperativity, and P50 is the oxygen partial pressure at 50% saturation. The sliders shift the effective P50 with a teaching approximation of the Bohr effect: lower pH, higher CO₂, and higher temperature increase P50 and shift the curve right, making unloading easier in active tissue. Higher affinity conditions shift the curve left. The second plot converts saturation into blood oxygen content C_O₂ = 1.34·Hb·S + 0.003·pO₂, separating the large hemoglobin-bound reservoir from the small dissolved oxygen contribution. Arterial and venous points show how changes in pO₂ and curve position affect saturation, content, and extracted oxygen.

Who it's for: Students in physiology, medicine, biophysics, or biomedical engineering learning blood gas transport, cooperative binding, and the Bohr effect.

Key terms

  • Hemoglobin saturation
  • Hill equation
  • P50
  • Bohr effect
  • Oxygen content
  • pO2
  • Cooperative binding
  • Oxygen extraction

This is a teaching model for adult hemoglobin. It omits fetal hemoglobin, dyshemoglobins, 2,3-BPG details, acid-base buffering, and full blood gas physiology.

Live graphs

O2-Hb dissociation

26.6 mmHg
2.8
7.4
37 °C
40 mmHg
15 g/dL
95 mmHg
40 mmHg

Bohr effect approximation: lower pH, higher CO2, and higher temperature increase effective P50 and shift the curve right. O2 content includes hemoglobin-bound and dissolved oxygen.

Measured values

effective P5026.6 mmHg
curve shiftnear standard curve
SaO2 / SvO297 / 76%
CaO2 / CvO219.8 / 15.4 mL/dL
extracted O24.5 mL/dL

How it works

Interactive oxygen-hemoglobin dissociation curve: Hill saturation, P50 shifts from pH/CO2/temperature, arterial and venous points, Bohr effect, and oxygen content.

Key equations

S = pO₂ⁿ/(P50ⁿ + pO₂ⁿ), C_O₂ = 1.34 Hb S + 0.003 pO₂. Lower pH / higher CO₂ / higher T raises P50 (right shift).

Frequently asked questions

What does P50 mean?
P50 is the pO₂ at which hemoglobin is 50% saturated. A higher P50 means lower affinity and a right-shifted curve; a lower P50 means higher affinity and a left-shifted curve.
Why does active tissue shift the curve right?
Active tissue tends to be warmer, more acidic, and richer in CO₂. These conditions stabilize the deoxygenated form of hemoglobin, raising P50 and helping oxygen unload where metabolism is high.
Why include oxygen content, not only saturation?
Saturation alone ignores hemoglobin concentration. An anemic patient can have high SaO₂ but low total oxygen content because there is less hemoglobin available to carry oxygen.