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B3.1 Gas exchangeIB Biology HL: Revision notes

Section 1

Size, exchange surfaces and gradients

As organisms grow, surface area-to-volume ratio falls and the distance from centre to surface rises, so large organisms need specialised gas-exchange surfaces. These are permeable, thin, moist and have a large surface area. In animals, gradients are kept steep by dense blood vessel networks, continuous blood flow and ventilation (air in lungs, water over gills).

Key termssurface area-to-volume ratioconcentration gradientventilation

Section 2

Mammalian lungs, ventilation and lung volumes

Adaptations: branched bronchioles, huge alveolar surface area, thin alveolus walls, extensive capillary beds, and surfactant to stop alveoli sticking together.

Inhalation: external intercostals raise the ribs; diaphragm contracts and flattens; volume up, pressure down, air in. Forced exhalation: internal intercostals lower the ribs; abdominal muscles push the diaphragm up.

Vital capacity = tidal volume + inspiratory reserve + expiratory reserve.

Key termssurfactantdiaphragmintercostal musclestidal volumevital capacity

Section 3

Leaves, transpiration and stomatal density

Leaf tissues from top: waxy cuticle, upper epidermis, palisade mesophyll, spongy mesophyll with air spaces, lower epidermis with stomata and guard cells; veins carry xylem and phloem. Transpiration is a consequence of gas exchange: open stomata let CO₂ in and water vapour out. Rate rises with temperature, light, air movement and lower humidity. Stomatal density = mean count ÷ πr²; repeat counts because biological material varies.

Key termswaxy cuticlespongy mesophyllstomatatranspirationstomatal density

Section 4

HL: Haemoglobin and cooperative binding

Each haemoglobin molecule has four polypeptides, each with a haem group that binds one O₂. Binding of the first O₂ changes the molecule's conformation, raising the affinity of the others: cooperative binding. Releasing one O₂ likewise makes the rest leave more easily.

Foetal haemoglobin has a higher affinity for oxygen than adult haemoglobin, so in the placenta it loads oxygen that maternal haemoglobin is releasing.

Key termshaem groupcooperative bindingfoetal haemoglobinaffinity

Section 5

HL: Oxygen dissociation curves

An oxygen dissociation curve plots percentage saturation of haemoglobin against partial pressure of oxygen. It is S-shaped (sigmoid) because of cooperative binding: a shallow start (first O₂ binds with difficulty), a steep middle, and a plateau at high partial pressures.

  • At the lungs (about 13 kPa) haemoglobin is almost fully saturated.
  • At respiring tissues (steep part) a small fall in partial pressure releases a lot of oxygen.
  • A curve to the left (foetal) means higher affinity; to the right means lower affinity.
Key termsoxygen dissociation curvepartial pressurepercentage saturation
Exam tip

Left = loads more readily (higher affinity). Right = unloads more readily (lower affinity).

Section 6

HL: The Bohr shift

Carbon dioxide binds to haemoglobin at allosteric sites (not the haem), changing its shape and lowering its affinity for oxygen. So in tissues with high CO₂, the curve shifts to the right and more oxygen dissociates: the Bohr shift. The benefit is that actively respiring tissues, which produce the most CO₂, receive the most oxygen.

Key termsBohr shiftallosteric binding
Common mistake

Carbon dioxide does not compete with oxygen for the haem groups; it binds allosterically elsewhere on the molecule.

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