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Myoglobin !

Myoglobin stores oxygen inside muscle; it has a single heme and gives it up only when oxygen falls very low.

Updated 2026-11-01

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Key facts

  • A single chain of 153 amino acids with eight helices (A–H) and one heme; it binds one O₂ molecule.
  • Hyperbolic saturation curve (no cooperativity); P50 about 2–3 mmHg versus about 26 mmHg for hemoglobin.
  • It is not affected by 2,3-BPG, CO₂ or pH (no Bohr effect).
  • The proximal histidine (F8) binds the iron; the distal one (E7) stabilises O₂ and lowers CO affinity.
Genes
MB
Structure (PDB)
3RGK

Structure

  • Structure 3RGK is human myoglobin (K45R variant, a surface change far from the heme) with its heme group.
  • It was the first protein whose 3D structure was solved by X-ray (Kendrew, 1958, sperm whale myoglobin).

Regulation

  • It is abundant in type I (red, oxidative) muscle fibres and in the heart; it rises with endurance training and altitude.

Inhibitors and toxins

  • Carbon monoxide (binds the heme iron)
  • Oxidants that turn Fe²⁺ into Fe³⁺ (metmyoglobin)

Clinical notes

  • Rhabdomyolysis: released myoglobin is filtered and damages the renal tubule (acute kidney injury); urine is dark and the dipstick is positive for blood without red cells.
  • It rises in blood 1–3 hours after muscle or heart injury; it is sensitive but not specific, which is why troponin replaced it for myocardial infarction.
  • Causes of rhabdomyolysis: crush injury, compartment syndrome, extreme exercise, seizures, statins, heat stroke.

Test yourself

Think of the answer, then tap the question to see it.

Why is the myoglobin curve hyperbolic and the hemoglobin curve sigmoid?

Myoglobin has a single binding site; hemoglobin has four that cooperate.

How does myoglobin harm the kidney in rhabdomyolysis?

It is filtered by the glomerulus, blocks the tubules, and its heme causes oxidative damage: acute kidney injury.

Which urine finding suggests myoglobinuria?

A dipstick positive for blood with no red cells under the microscope.

Does myoglobin respond to 2,3-BPG?

No: it is a monomer with no central cavity; 2,3-BPG acts only on hemoglobin.

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Educational information, not medical advice. For any symptom, see a health professional.

Sources: MB: Myoglobin (human) (UniProt, 2026); 3RGK: Crystal Structure of Human Myoglobin Mutant K45R (RCSB Protein Data Bank, 2026); Myoglobin blood test: MedlinePlus Medical Encyclopedia (MedlinePlus, US National Library of Medicine, 2026); Textbook of Biochemistry for Medical Students, 6th ed. (Jaypee Brothers Medical Publishers (Vasudevan DM, Sreekumari S, Vaidyanathan K), 2011).

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Representative model, for educational purposes only.