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Hemoglobin vs Myoglobin: Structure, Oxygen Affinity and Curves
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Myoglobin stores oxygen in muscle. Hemoglobin transports oxygen in blood. Their different structures give them different binding curves.
Comparison
| Myoglobin | Hemoglobin | |
|---|---|---|
| Location | Muscle | Red blood cells |
| Structure | Monomer, one heme | Tetramer (2 alpha, 2 beta), four hemes |
| Curve | Hyperbolic | Sigmoidal |
| Cooperativity | None | Positive |
| O2 affinity | Higher (lower P50) | Lower (higher P50) |
| Regulated by H+, CO2, 2,3-BPG | No | Yes |
| Role | Storage and release in working muscle | Loading in lungs, unloading in tissues |
Why the curves differ
Hemoglobin shifts between a low-affinity T state and a high-affinity R state. Binding one O2 favors the R state, so the next oxygens bind more easily. That cooperativity gives the S shape.
Myoglobin has a single binding site, so each molecule binds oxygen independently, giving a hyperbola.
Why it makes sense physiologically
- In the lungs, high pO2 loads hemoglobin nearly fully.
- In tissues, hemoglobin gives up oxygen over a range of pO2.
- Myoglobin holds oxygen more tightly and releases it mainly when pO2 falls very low, as in exercising muscle.
Fetal hemoglobin
Fetal hemoglobin has a higher O2 affinity than adult hemoglobin because it binds 2,3-BPG less strongly. Oxygen therefore moves from maternal to fetal blood.
Common traps
- Giving myoglobin a sigmoidal curve.
- Saying myoglobin is lower affinity. It binds oxygen more tightly.
- Applying Bohr or 2,3-BPG effects to myoglobin.
One-minute recap
- Myoglobin: monomer, hyperbolic, higher affinity, storage.
- Hemoglobin: tetramer, sigmoidal, cooperative, transport.
Check yourself: 5-question mini-quiz
1. What is the shape of the myoglobin binding curve?
Hyperbolic.
2. Why is the hemoglobin curve sigmoidal?
Positive cooperativity as binding shifts the protein from the T state toward the R state.
3. Which has the higher oxygen affinity, myoglobin or hemoglobin?
Myoglobin.
4. How many heme groups does hemoglobin carry?
Four.
5. Why does fetal hemoglobin bind oxygen more tightly than adult hemoglobin?
It binds 2,3-BPG less strongly.
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