Gas transport in blood
CIE A-Level BiologyΒ· 8.3 (d) Gas transport in bloodΒ· 15 min read
1. Oxygen Transport by Haemoglobinβ β ββββ± 4 min
Oxyhaemoglobin
A reversible compound formed when oxygen binds to the haem group of haemoglobin in red blood cells. Binding occurs in the lungs where is high.
Example:
Each haemoglobin molecule can bind up to 4 oxygen molecules, forming .
Haemoglobin has a high affinity for oxygen when is high, which occurs in the alveoli of the lungs. Oxygen diffuses down its concentration gradient from the alveoli into red blood cells, where it binds to haemoglobin for transport. In respiring tissues, is low, so haemoglobin releases (unloads) oxygen, which diffuses into tissue cells to support respiration.
Explain why an increase in the rate of cellular respiration leads to more oxygen being unloaded from haemoglobin to muscle tissue.
- 1
- Increased respiration increases oxygen consumption, so in muscle tissue falls.
- 2
- Higher respiration also produces more , which lowers blood pH (the Bohr effect).
- 3
- Lower pH reduces haemoglobin's affinity for oxygen.
- 4
- This shifts the oxygen dissociation curve to the right, meaning more oxygen is unloaded at a given to meet the increased demand of the muscle.
2. Forms of Carbon Dioxide Transportβ β ββββ± 4 min
Carbon dioxide is transported in the blood in three different forms, in varying proportions:
~5% dissolved directly in blood plasma
~10% bound to the amino groups of haemoglobin, forming carbaminohaemoglobin
~85% transported as hydrogencarbonate ions () in plasma
Carbonic anhydrase
A zinc-based enzyme found in high concentrations in red blood cells that catalyses the reversible reaction between carbon dioxide and water to form carbonic acid.
Calculate how much COβ is transported as hydrogencarbonate ions in 1 dmΒ³ of blood that contains 2.5 cmΒ³ of dissolved COβ and 0.5 cmΒ³ of COβ bound as carbaminohaemoglobin, if total blood COβ is 25 cmΒ³.
- 1
- Total COβ in the sample is given as 25 cmΒ³.
- 2
- Add COβ transported by other methods: cmΒ³.
- 3
- Subtract to get COβ as : cmΒ³.
- 4
- Check the proportion: , which matches the expected ~85% range.
3. Chloride Shift and Buffering Actionβ β β βββ± 5 min
When carbon dioxide diffuses into red blood cells, carbonic anhydrase catalyses its combination with water to form carbonic acid (). Carbonic acid quickly dissociates into hydrogen ions () and hydrogencarbonate ions ():
Hydrogencarbonate ions diffuse out of the red blood cell into the plasma down their concentration gradient. To maintain electrical neutrality, chloride ions () diffuse from the plasma into the red blood cell: this movement is called the chloride shift.
The hydrogen ions produced would lower the pH of the red blood cell if they were not buffered. Haemoglobin acts as a buffer by binding to the hydrogen ions to form haemoglobinic acid, which prevents a damaging drop in intracellular pH.
Explain why the chloride shift is necessary for continued COβ transport in blood.
- 1
- When COβ enters the red blood cell, it dissociates into and .
- 2
- Negatively charged leaves the red blood cell down its concentration gradient.
- 3
- This loss of negative charge leaves the red blood cell with a net positive charge.
- 4
- Negatively charged chloride ions move into the cell from plasma to balance the net charge, allowing to continue diffusing out and COβ to keep entering the cell.
4. The Bohr Effectβ β β βββ± 4 min
The Bohr effect describes how increasing (and decreasing pH) reduces haemoglobin's affinity for oxygen. This shifts the oxygen dissociation curve to the right, meaning that haemoglobin releases more oxygen at a given .
This is a key adaptation that matches oxygen supply to tissue demand: highly active tissues (e.g. contracting muscle) produce more , which lowers pH, triggering more oxygen unloading exactly where it is needed most.
Test your understanding of the Bohr effect:
Which of the following correctly describes the effect of high on haemoglobin?
Increased affinity for oxygen, more unloading
Decreased affinity for oxygen, more unloading
Increased affinity for oxygen, less unloading
Decreased affinity for oxygen, less unloading
Reveal answer
1 βCorrect: High lowers pH, reduces affinity, so more oxygen is released to tissues.
Where would you expect the most right-shifted dissociation curve?
Alveoli
Resting leg muscle
Active heart muscle
Brain at rest
Reveal answer
2 βCorrect: Active heart muscle has very high COβ production and low , so maximum shift right.
5. Common Pitfalls
Wrong move:
Stating that COβ is mostly carried as carbon dioxide in plasma.
Why:
Only 5% of COβ is dissolved in plasma; 85% is carried as hydrogencarbonate ions.
Correct move:
State that 85% of carbon dioxide is transported as hydrogencarbonate ions in plasma.
Wrong move:
Claiming the chloride shift moves chloride ions out of red blood cells.
Why:
Hydrogencarbonate moves out; chloride moves in to balance charge.
Correct move:
Chloride ions diffuse into red blood cells during the chloride shift.
Wrong move:
Saying haemoglobin binds to COβ to make oxyhaemoglobin.
Why:
Oxyhaemoglobin is haemoglobin bound to oxygen. COβ binds to haemoglobin to form carbaminohaemoglobin.
Correct move:
Oxygen binds to haem groups to form oxyhaemoglobin; COβ binds to amino groups to form carbaminohaemoglobin.
Wrong move:
Thinking the Bohr effect shifts the dissociation curve to the left.
Why:
A left shift means higher affinity for oxygen, which does not match the needs of active tissues.
Correct move:
Increased COβ reduces affinity, shifting the curve to the right, increasing oxygen unloading.
Wrong move:
Stating that carbonic anhydrase only catalyses reactions in respiring tissues.
Why:
The reaction is reversible, and the enzyme catalyses the breakdown of carbonic acid to COβ and water in the lungs too.
Correct move:
Carbonic anhydrase catalyses the reversible interconversion of COβ + water and carbonic acid in both tissues and lungs.
6. Quick Reference Cheatsheet
Process | Key Location | Key Fact |
|---|---|---|
Oxygen loading | Alveoli (lungs) | High β Hb binds Oβ β oxyhaemoglobin |
Oxygen unloading | Respiring tissues | Low + high β Hb releases Oβ |
Most COβ transport | Plasma | ~85% as hydrogencarbonate ions () |
Carbonic anhydrase | Red blood cells | Catalyses |
Chloride shift | RBC membrane | moves into RBC to balance charge |
Bohr effect | Active tissues | High β lower pH β lower Hb affinity β right shift |
pH buffering | Red blood cells | Hb binds to prevent damaging pH drop |
When this came up on past exams
AI-estimated based on syllabus patterns β cross-check with official past papers for accuracy. Use only as revision-focus signals.
- 2022 Β· 22
Describe CO2 transport in RBCs
- 2023 Β· 12
Explain oxygen dissociation curve shift
- 2021 Β· 21
Outline chloride shift process
Going deeper
What's Next
Understanding gas transport in blood connects alveolar gas exchange to cellular respiration, and explains how the body adapts to changing metabolic demand during exercise. The principles of haemoglobin oxygen affinity also underpin comparisons between fetal and adult haemoglobin, and adaptations to high altitude. This sub-topic completes the core understanding of blood function in mammalian transport, and leads into the structure of blood vessels and regulation of the circulatory system that make up the rest of this unit. Mastering this content is also critical for exam questions on gas exchange and respiration across multiple topics.
