Key Inorganic Ions and Their Roles Revision Notes | A Level AQA Biology
Iron(II) ions in haemoglobin bind oxygen, sodium ions drive co-transport of glucose, and hydrogen ions set pH. Free AQA notes and 13 questions answered.
Updated 5 Sept 2026 · Revise Right Team
Key Inorganic Ions and Their Roles is part of Inorganic ions in A Level AQA Biology.
7 min
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A Level AQA
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What this lesson covers
Iron(II) ions in haemoglobin bind oxygen, sodium ions drive co-transport of glucose, and hydrogen ions set pH. Free AQA notes and 13 questions answered.
State the roles of hydrogen ions, iron ions, sodium ions, and phosphate ions in biological systems
Explain how each inorganic ion contributes to a specific biological process or molecule
Compare the structural and functional roles of phosphate ions in DNA and ATP
Apply knowledge of ion roles to unfamiliar biological contexts in exam questions
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Use this lesson to stay inside Inorganic ions while connecting the detail back to the wider Biological molecules topic.
Inorganic ion: A charged atom or group of atoms of non-biological origin that plays a functional role in biological processes. Present in solution inside and outside cells.
Haemoglobin: A globular protein in red blood cells that transports oxygen. Contains iron(II) ions (Fe²⁺) within haem groups that reversibly bind oxygen molecules.
Co-transport: A membrane transport mechanism in which the movement of one substance (sodium ions) down its concentration gradient drives the active uptake of another substance (glucose or amino acids) against its gradient.
Phosphate ion: An inorganic ion ($\text{PO}_4^{3-}$) that forms part of the sugar-phosphate backbone of DNA and the high-energy bonds of ATP. Central to both information storage and energy transfer.
Revision notes
Read the core explanations from Key Inorganic Ions and Their Roles before testing yourself from memory.
1. Why Inorganic Ions Matter
Your body contains dozens of different ions, and without them, almost nothing works. Oxygen would not be carried in the blood, glucose could not enter intestinal cells, and DNA could not hold its shape. Four ions sit at the heart of the AQA specification: hydrogen ions ($\text{H}^+$), iron ions ($\text{Fe}^{2+}$), sodium ions ($\text{Na}^+$), and phosphate ions ($\text{PO}_4^{3-}$).
Each ion has a precise, exam-testable role. The goal of this lesson is to connect each ion to its biological context so clearly that you can explain, compare, and apply that knowledge under exam conditions.
2. Hydrogen Ions and pH
pH is a measure of hydrogen ion concentration. The lower the pH, the higher the concentration of $\text{H}^+$ ions in solution. This relationship is logarithmic: a drop of one pH unit represents a tenfold increase in $\text{H}^+$ concentration.
Why does this matter biologically? Enzymes are proteins whose active sites depend on a precise three-dimensional shape. Hydrogen ions interact with the R-groups of amino acids, altering the charges and hydrogen bonding that maintain that shape. A shift in $\text{H}^+$ concentration can denature an enzyme or reduce its affinity for its substrate — which is why blood pH is tightly regulated between 7.35 and 7.45.
Hydrogen ions are also directly involved in ATP synthesis. During oxidative phosphorylation, $\text{H}^+$ ions are pumped across the inner mitochondrial membrane, creating a concentration gradient. Their movement back through ATP synthase drives the phosphorylation of ADP to ATP — a process called chemiosmosis. The hydrogen ion gradient is the driving force.
3. Iron Ions and Haemoglobin
Haemoglobin is a quaternary protein made of four polypeptide chains, each containing a haem group. At the centre of each haem group sits a single iron(II) ion, $\text{Fe}^{2+}$. This ion is the actual site where oxygen binds.
One haemoglobin molecule contains four haem groups, so it can carry up to four oxygen molecules simultaneously. The binding is reversible: in the lungs, where oxygen partial pressure is high, $\text{Fe}^{2+}$ binds oxygen to form oxyhaemoglobin. In respiring tissues, where oxygen partial pressure is low, oxygen is released and haemoglobin is regenerated.
The iron ion does not change its oxidation state during normal oxygen transport — it remains $\text{Fe}^{2+}$ throughout. This is worth noting because carbon monoxide binds to the same $\text{Fe}^{2+}$ site with a much higher affinity than oxygen (about 200 times greater), very strongly blocking it and effectively preventing oxygen transport. That is why carbon monoxide poisoning is so dangerous.
Iron deficiency leads to anaemia — a condition in which there are insufficient functional haemoglobin molecules to carry adequate oxygen. Symptoms include fatigue and breathlessness, directly reflecting the reduced oxygen delivery to tissues. This clinical consequence illustrates how a single ion underpins a critical physiological function.
4. Sodium Ions and Co-transport of Glucose and Amino Acids
Glucose and amino acids are too large and too polar to cross the phospholipid bilayer by simple diffusion. In the epithelial cells lining the small intestine, their absorption depends on a co-transport mechanism that exploits the sodium ion gradient.
Here is how the system works. The sodium-potassium pump ($\text{Na}^+/\text{K}^+$ ATPase) on the basolateral membrane uses ATP to actively transport sodium ions out of the epithelial cell. This keeps the intracellular sodium concentration low. On the apical (lumen-facing) membrane, a co-transporter protein couples the movement of $\text{Na}^+$ down its concentration gradient into the cell with the simultaneous movement of glucose or an amino acid against its concentration gradient into the cell.
The sodium ion gradient is the energy source for glucose and amino acid uptake. The $\text{Na}^+$ ions effectively 'pull' the nutrient molecules into the cell. Once inside, glucose and amino acids leave the epithelial cell via facilitated diffusion through the basolateral membrane into the blood. Sodium ions are continuously recycled by the pump to maintain the gradient.
Worked example: Tracing the Co-transport Pathway for Glucose
Describe, in sequence, how a glucose molecule moves from the intestinal lumen into the blood, with reference to sodium ions.
$\text{Na}^+/\text{K}^+$ ATPase pumps $\text{Na}^+$ out of the epithelial cell using ATP hydrolysis. — This creates a low intracellular $\text{Na}^+$ concentration — the essential precondition for co-transport.
$\text{Na}^+$ moves down its concentration gradient into the cell via the co-transporter protein, carrying glucose with it against glucose's concentration gradient. — The energy stored in the $\text{Na}^+$ gradient (generated by ATP) drives glucose uptake. This is secondary active transport.
Glucose leaves the epithelial cell through carrier proteins on the basolateral membrane, moving down its concentration gradient into the blood capillary. — No energy is required at this step — the glucose concentration inside the cell is now higher than in the blood.
$\text{Na}^+$ that entered the cell is pumped back out by $\text{Na}^+/\text{K}^+$ ATPase, maintaining the gradient for continued co-transport. — Without this recycling, the gradient would dissipate and co-transport would cease.
Answer: Glucose moves from the lumen into the epithelial cell via co-transport with $\text{Na}^+$ (secondary active transport), then exits into the blood by facilitated diffusion. The $\text{Na}^+$ gradient, maintained by the $\text{Na}^+/\text{K}^+$ ATPase, provides the driving force.
5. Phosphate Ions in DNA and ATP
Phosphate ions ($\text{PO}_4^{3-}$) appear in two of the most important molecules in biology: DNA and ATP. Their role in each is structurally and functionally distinct, which makes this a favourite area for compare-style exam questions.
In DNA, each nucleotide contains a deoxyribose sugar, a nitrogenous base, and a phosphate group. The phosphate group of one nucleotide forms a covalent bond with the sugar of the next, creating the sugar-phosphate backbone. This backbone runs along the outside of the double helix, providing structural stability and directionality (the 5' to 3' orientation). The negative charges on the phosphate groups also repel each other, which — combined with the hydrogen bonds between complementary bases — contributes to the overall architecture of the molecule.
In ATP (adenosine triphosphate), three phosphate groups are linked in sequence to the adenosine unit. The bonds between the phosphate groups—called phosphoanhydride bonds—are high-energy bonds, with the terminal one (between the second and third phosphates) most frequently hydrolysed in cells. Hydrolysis of any phosphoanhydride bond releases energy, but the terminal bond is the one typically broken to form ADP and inorganic phosphate ($\text{P}_i$). The phosphate ion released ($\text{P}_i$) can also be transferred to another molecule in a process called phosphorylation, activating that molecule.
Feature
Phosphate in DNA
Phosphate in ATP
Location in molecule
Sugar-phosphate backbone
Three phosphate groups attached to adenosine
Type of bond formed
Covalent phosphodiester bond
High-energy phosphoanhydride bond
Primary role
Structural — maintains backbone integrity and directionality
Energy currency — releases energy on hydrolysis
Number of phosphate groups per monomer
One per nucleotide
Three per ATP molecule
What happens when bond breaks
Strand is cleaved (e.g. during restriction)
Energy released; ADP + $\text{P}_i$ formed
A key point for exam answers: phosphate ions are structural components of DNA (forming the backbone) and functional components of ATP (storing and releasing energy). These are different roles, and conflating them will cost marks.
6. Bringing the Four Ions Together
Now that each ion has been examined individually, it is worth stepping back to see the pattern. Each ion is effective precisely because of its charge and its ability to interact with specific biological molecules or proteins. The charge on $\text{H}^+$ disrupts enzyme tertiary structure; the $\text{Fe}^{2+}$ in haem provides a reversible binding site for oxygen; the $\text{Na}^+$ gradient powers nutrient uptake; and the $\text{PO}_4^{3-}$ group both scaffolds DNA and stores energy in ATP.
7. Exam Technique and Common Mistakes
Questions on inorganic ions tend to use command words such as 'explain', 'describe', 'compare', and 'suggest'. Each demands a different response structure. For 'explain' questions, always include a mechanism — not just a statement of what happens, but why it happens at the molecular or ionic level.
For 'compare' questions on phosphate ions in DNA versus ATP, structure your answer around named similarities and differences. Both molecules contain phosphate groups covalently bonded to a sugar; the key difference is that in DNA the phosphate is structural, whereas in ATP it is functional (energy storage and transfer). Stating both sides explicitly is what earns the marks.
Sources and content standards
Published by Revise Right. Use the official specification reference to check the requirements for your course. Content updated: 2026-09-05.
Carbon monoxide is dangerous because it binds to the same iron(II) site in haemoglobin as oxygen, with an affinity about 200 times greater than oxygen. This very strongly blocks the site and effectively prevents oxygen transport around the body.
What is secondary active transport?
Secondary active transport is the uptake of a molecule against its concentration gradient using energy stored in another ion's gradient rather than ATP directly. In the small intestine, Na⁺ moving down its gradient into epithelial cells carries glucose with it, and that Na⁺ gradient is maintained by the Na⁺/K⁺ ATPase using ATP.
What is the normal pH of blood?
Blood pH is tightly regulated between 7.35 and 7.45. This matters because hydrogen ions interact with the R-groups of amino acids, and a shift in H⁺ concentration can denature an enzyme or reduce its affinity for its substrate.
What is the role of hydrogen ions in biology?
pH is a measure of hydrogen ion concentration: the higher the H+ concentration, the lower the pH. They interact with the R-groups of amino acids, so changes in H+ concentration can denature enzymes. A hydrogen ion gradient across the inner mitochondrial membrane also drives ATP synthesis through ATP synthase, a process called chemiosmosis.
What is the role of iron ions in haemoglobin?
Each haem group in haemoglobin contains an iron(II) ion, which is the site where oxygen binds. The binding is reversible: oxygen binds in the lungs to form oxyhaemoglobin and is released in respiring tissues. With four haem groups, one haemoglobin molecule can carry up to four oxygen molecules.
How do sodium ions help absorb glucose?
Sodium ions drive the co-transport of glucose and amino acids into epithelial cells of the small intestine. The sodium-potassium pump keeps the sodium concentration inside the cell low, so sodium ions move in through a co-transporter protein down their concentration gradient, carrying glucose with them against its concentration gradient.
What is the role of phosphate ions in DNA and ATP?
In DNA, phosphate ions form the sugar-phosphate backbone through covalent phosphodiester bonds, a structural role. In ATP, three phosphate groups are linked by high-energy phosphoanhydride bonds, and hydrolysis of the terminal bond releases energy, a functional role. Released inorganic phosphate can also be transferred to another molecule by phosphorylation, activating it.
What is pH?
pH is a logarithmic scale that measures the concentration of hydrogen ions (H⁺) in a solution. A pH of 7 is neutral, lower values are acidic with a higher H⁺ concentration, and a drop of one pH unit represents a tenfold increase in H⁺ concentration.
What is iron deficiency anaemia?
Iron deficiency anaemia is a condition in which there are insufficient functional haemoglobin molecules to carry adequate oxygen. Symptoms include fatigue and breathlessness, directly reflecting the reduced oxygen delivery to tissues.
How many oxygen molecules can one haemoglobin carry?
One haemoglobin molecule can carry up to four oxygen molecules, because it has four haem groups, each with a single iron(II) ion at its centre where oxygen binds. The binding is reversible: oxygen binds in the lungs and is released in respiring tissues.
How does glucose get from intestinal epithelial cells into the blood?
Glucose leaves intestinal epithelial cells by facilitated diffusion through carrier proteins on the basolateral membrane, moving down its concentration gradient into the blood capillary. No energy is needed at this step because glucose concentration inside the cell is now higher than in the blood.
Why can't glucose cross the cell membrane by simple diffusion?
Glucose and amino acids are too large and too polar to cross the phospholipid bilayer by simple diffusion. In the small intestine their absorption therefore depends on a co-transport mechanism that exploits the sodium ion gradient.
Does the iron ion change when haemoglobin carries oxygen?
The iron ion in haemoglobin does not change its oxidation state during normal oxygen transport; it remains Fe²⁺ throughout. Oxygen binds reversibly to Fe²⁺ in the lungs, where oxygen partial pressure is high, and is released in respiring tissues, where it is low.