AQA A LEVEL BIOLOGY

TOPIC 1: BIOLOGICAL MOLECULES

NOTES
 1.1 Monomers and Polymers – 1.2 Carbohydrates
MONOMERS AND POLYMERS
MONOMER: smaller units from which larger
molecules are made
 E.g., monosaccharides, amino acids,
nucleotides
POLYMER: molecules made from many
monomers joined together
 E.g., polysaccharides, proteins, DNA/RNA
CONDENSATION AND HYDROLYSIS
CONDENSATION REACTIONS:
 Join 2 molecules together
 Eliminates a water molecule
 Forms a chemical bond
HYDROLYSIS REACTIONS:
 Separates 2 molecules
 Requires water molecule
 Breaks a chemical bond
SACCHARIDES
MONOSACCHARIDES: monomer from which
larger carbohydrates are made
 E.g., glucose, fructose, galactose
DISACCHARIDES: formed from condensation of
two monosaccharides
 E.g., maltose, sucrose, lactose
 Maltose is formed from two a-glucose
molecules
 Sucrose is formed from glucose and
fructose
 Lactose is formed from glucose and
galactose
POLYSACCHARIDES: formed from condensation
of many monosaccharides
The formation of disaccharides and
polysaccharides from condensation reactions
forms a glycosidic bond between each molecule
STRUCTURE OF GLUCOSE
 Monosaccharide
 Hexose (6-carbon) sugar
 Can adopt different isoforms (a- and b-
glucose)
 A-glucose: hydrogen is above carbon ring
 B-glucose: hydrogen is below carbon ring
TEST FOR REDUCING SUGARS
REDUCING SUGARS: a sugar that can donate
electrons to reduce another chemical compound
(e.g. all monosaccharides and some
disaccharides like maltose/lactose)
Reducing sugars are tested using Benedict’s
reagent:
 Add 2cm3 of the sample to a test tube (grind
in water if not in liquid form)
 Add an equal volume of Benedict’s reagent
 Heat the mixture in a gently boiling water
bath for 5 minutes
 If a reducing sugar is present, colour will
change to green, yellow, orange or red
depending on concentration of reducing
sugar present
TEST FOR NON-REDUCING SUGARS
Other disaccharides such as sucrose are non-
reducing sugars which do not change the colour
of Benedict’s reagent when heated with it.
To detect a non-reducing sugar:
 Add 2 cm3 of the sample to a test tube with
the same volume of Benedict’s reagent
 Place the test tube in a gently boiling water
bath for 5 minutes
 If the solution has not changed colour, a
non-reducing sugar is present
 Add another 2cm3 of the same sample to
2cm3 of hydrochloric acid
o This will hydrolyse any disaccharides
present into monosaccharides
 Slowly add sodium hydrogencarbonate to
neutralise the hydrochloric acid
o Benedict’s reagent does NOT work in
ACIDIC conditions
 Re-test the resulting solution by heating it
with 2cm3 of Benedict’s reagent in a water
bath for 5 mins
 If a non-reducing sugar was present, the
solution should now turn from blue to
orange-brown
o This is due to the reducing sugars
present upon hydrolysis of the non-
reducing sugar
POLYSACCHARIDES
Polysaccharides are polymers of
monosaccharides joined together by glycosidic
bonds formed by condensation reaction
 They are large and thus insoluble
 Their insolubility makes them suitable for
storage
 When hydrolysed, they produce mono-
/disaccharides which can be used in
respiration
STARCH
STRUCTURE OF STARCH:
 Chains of a-glucose monosaccharides linked
by 1,4-glycosidic bonds formed by
condensation reactions
 Unbranched or branched chains
 Unbranched chains are wound into tight
coils that make the molecule very compact
STRUCTURE RELATED TO FUNCTION:
 Insoluble so osmotically inactive
o Does not affect water potential of cells
 Helical so compact
o Can be stored in small spaces
 Large so cannot diffuse out of cells
 Can be highly branched which gives large
surface area for enzymes to work on
o Enzymes can hydrolyse it into a-glucose
for aerobic respiration
TEST FOR STARCH
 Place 2cm3 of the sample into a test tube or
on a spotting tile
 Add two drops of iodine solution and shake
or stir
 The presence of starch is indicated by a
blue-black colouration
GLYCOGEN
STRUCTURE OF GLYCOGEN:
 Similar to starch but has shorter chains and
is more highly branched
 Major carbohydrate storage product of
animals
STRUCTURE RELATED TO FUNCTION:
 Insoluble so osmotically inactive
o Does not affect water potential of cells
 Large and insoluble so cannot leave cells
 Highly branched gives large surface area for
enzymes to work on
o Can hydrolyse it into a-glucose for
aerobic respiration
 Compact so can be stored in small spaces
CELLULOSE
STRUCTURE OF CELLULOSE:
 Made up of B-glucose monomers
 Forms straight unbranched chains which
run parallel to one another
o Allows hydrogen bonds to form cross-
linkages between adjacent chains
 Cellulose chains are grouped together to
form microfibrils which arrange in parallel
groups to form fibres
STRUCTURE RELATED TO FUNCTION:
 Long, straight, unbranched chains run
parallel to each other
 Hydrogen bonds allow formation of cross-
links which provide strength and rigidity to
cell wall
 Prevents cell from bursting as water enters
in by osmosis
 1.3. Lipids
TYPES OF LIPIDS
Lipids are substances that share the following
features:
 Contain carbon, hydrogen and oxygen
 Proportion of oxygen to carbon and
hydrogen is smaller than in carbohydrates
 Insoluble in water
 Soluble in organic solvents
The main groups of lipids are triglycerides and
phospholipids.
ROLES OF LIPIDS
 Source of energy: when oxidised, lipids
provide 2x more energy than carbohydrates
 Insulation: fat store, prevents heat loss from
organism
 Protection: stored around delicate organs
 Waterproofing: lipids insoluble in water
TRIGLYCERIDES
STRUCTURE AND FEATURES OF TRIGLYCERIDES:
 Made up of one molecule of glycerol and 3
fatty acids joined by ester bonds formed in
condensation reactions
 Fatty acids can either be saturated or
unsaturated
 Saturated lipids are found in animal fats and
do not contain carbon-carbon double bonds
 Unsaturated lipids are found in plants and
contain carbon-carbon double bonds
o This allows the molecule to be able to
bend
o Unsaturated fats cannot pack together as
tightly due to the double bond and are
therefore liquid at room temperature
STRUCTURE RELATED TO FUNCTION:
 High ratio of energy-storing carbon-
hydrogen bonds to carbon atoms
o Good source of energy
 High mass to energy ratio
o More energy can be stored in smaller
masses
 High H to O ratio
o Important source of water
 Large so insoluble
o Does not affect water potential of cells
PHOSPHOLIPIDS
STRUCTURE AND FEATURES OF PHOSPHOLIPIDS:
 In phospholipids, one of the fatty acids of a
triglyceride is substituted by a phosphate-
containing group
 Phosphate heads are hydrophilic (love
water) and fatty acid tails are hydrophobic
(hate water)
 In contact with water, phospholipids form a
bilayer or micelles
 They are polar molecules
STRUCTURE RELATED TO FUNCTION:
 Phospholipids are polar molecules which
means in an aqueous environment, they
form a bilayer within cell-surface
membranes
o Therefore a hydrophobic barrier is
formed between the inside and outside of
a cell
 The hydrophilic phosphate heads help to
hold at the surface of the cell-surface
membrane
 The structure of a phospholipid allows them
to form glycolipids by combining with
carbohydrates within the cell-surface
membrane
o These are important in cell recognition
EMULSION TEST
 Add 2cm3 of the sample to a grease-free
test tube and 5cm3 of ethanol
 Shake the tube thoroughly to dissolve any
lipid
 If a lipid is present, a cloudy white colour is
observed
 As a control, repeat with water as the
sample – the final solution should remain
clear
 1.4.1 Proteins
 A change in a single amino acid will lead to a
STRUCTURE OF AN AMINO ACID change in the protein’s shape and therefore
function
Amino acids are the basic monomer units that
form polypeptides. There are 20 naturally
occurring amino acids in proteins.
Each amino acid has a central carbon atom to
which 4 different chemical groups are attached:
 Amino group (-NH2)
 Carboxyl group (-COOH)
 Hydrogen atom
 R (side) group – variable between each
SECONDARY STRUCTURE
amino acid The secondary structure is the 3D folding of a
polypeptide chain. It can form either alpha
helices or beta pleated sheets.
 The H of the -NH has a slight positive charge
which attracts the slight negative charge on
the O of the -COOH
o As a result weak hydrogen bonds form
between them
 This causes the long polypeptide chain to be
FORMATION OF A PEPTIDE BOND folded into a 3D shape
Two amino acids can join together in a
condensation reaction to form a dipeptide.
The OH from the carboxyl group combines with
the H from the amino group to produce water and
links the two amino acids by a peptide bond.

STRUCTURAL LEVELS OF PROTEINS
The structure of proteins is determined by the
order and number of amino acids, the bonding
present, and the shape of the protein.
PRIMARY STRUCTURE
The primary structure is the sequence of amino
acids in a polypeptide chain. Many amino acid
monomers join together in a polymerisation
reaction to form a polypeptide.
 The order of amino acids determines a
proteins ultimate shape and thus function
TERTIARY STRUCTURE
The 3D structure of a protein can be twisted and
folded further to give a specific 3D shape.
This is maintained by multiple different bonds
whose position depend on the primary structure
of the protein.
 Disulfide bonds – fairly strong and not easily
broken
o Form between two cysteines
 Ionic bonds – formed between any carboxyl
and amino group not involved in peptide
bond formation
o They are weaker than disulfide bonds and
are easily broken by changes in pH
 Hydrogen bonds – numerous but easily
broken
 o Lots of the amino acid glycine helps
close packing
 TERTIARY: chain is twisted into second helix
 QUATERNARY: three of these polypeptide
chains are wound together in a helix

QUATERNARY STRUCTURE
The quaternary structure arises when there is
more than one polypeptide chain.
There can also be prosthetic (non-protein)
groups, such as the iron-containing haem group
in haemoglobin.

TEST FOR PROTEINS

The Biuret test is used to detect the presence of
peptide bonds.
 Add the sample in a test tube and add an
equal volume of sodium hydroxide solution
 Add a few drops of dilute copper sulfate
solution and mix gently
 The presence of peptide bonds and hence a
protein is indicated by a colour change from
blue to purple
 The sample will stay blue if no protein is
present

PROTEIN SHAPE AND FUNCTION

There are two basic types of proteins, whose
roles depend on their molecular shape:
 Fibrous proteins (e.g. collagen) have
structural functions
 Globular proteins (e.g. haemoglobin,
enzymes) have metabolic functions

FIBROUS PROTEINS
Fibrous proteins form long chains which run
parallel to each other. These chains are linked by
cross-bridges which forms stable molecules.
One example of a fibrous protein is collagen:
 PRIMARY: unbranched polypeptide chain
 SECONDARY: polypeptide chain is tightly
wound
 1.4.2 Enzyme Action
ENZYMES AS CATALYSTS
Enzymes are globular proteins that act as
catalysts.
CATALYSTS: substance that can increase the rate
of reaction by providing an alternative reaction
pathway with a lower activation energy
ENZYME STRUCTURE
Since enzymes are globular proteins, they have a
specific 3D shape that is the result of their amino
acid sequence.
The active site is a functional region of the
enzyme.
 It is made up of a relatively small number of
amino acids
 It forms a small depression within the
enzyme molecule
The substrate is the molecule on which the
enzyme acts on.
 It fits into the active site and forms the
enzyme-substrate complex
 It is held within the active site by bonds that
temporarily form between certain amino
acids of the active site and substrate
 The enzyme is flexible and can mould itself
around the substrate
 As the enzyme changes shape, the enzyme
puts a strain on the substrate molecule
 This strain distorts a particular bond or
bonds in the substrate
 This lowers the activation energy needed to
break the bond and starts the reaction
The induced fit model is the most recent and
widely accepted model of enzyme action.
LOCK AND KEY
The lock and key model proposes that the active
site of the enzyme is completely complementary
to the substrate and fits the substrate exactly.
 The active site is a fixed shape and doesn’t
change
o It is complementary to one specific
substrate
 After a successful collision, an enzyme-
substrate complex forms leading to a
reaction
This model is old and outdated and has been
refuted by the induced fit model.

MODELS OF ENZYME ACTION

There are two models of enzyme action that
describe how substrates fit into active sites to
start a reaction.
 Induced fit model
 Lock and key model

INDUCED FIT MODEL

The induced fit model proposes that the active
site forms as the enzyme and substrate interact.
 Before reacting, the enzyme’s active site is
not completely complementary to substrate
 1.4.3 Factors affecting enzyme action
MEASURING ENZYME-CATALYSED
REACTIONS
There are two changed most frequently
measured when measuring the progress of an
enzyme-catalysed reaction:
 The formation of products
 The disappearance of substrate
Generally for both measurements:
 At first, there is a lot of substrate so many
substrate molecules can come into contact
with the empty active sites
 Therefore all enzyme active sites are filled
at any given moment so the substrate is
rapidly broken down into product
 The amount of substrate decreases as it is
broken down, resulting in an increase in the
amount of product
 As the reaction proceeds, it becomes more
difficult for substrate molecules to come
into contact with active sites as there are
fewer substrate molecules and more
product molecules which block them from
reaching the active site
 Therefore, it takes longer for the substrate
to be broken down so its rate of
disappearance slows and the rate of product
formation also slows
 The graph eventually flattens out as the
substrate has been used up
FACTORS AFFECTING RATE OF ENZYME-
CONTROLLED REACTION
The following factors affect the rate of enzyme-
controlled reactions:
 Temperature
 pH
 Enzyme concentration
 Substrate concentration
 Concentration of competitive and non-
competitive inhibitors
EFFECT OF TEMPERATURE
 Increasing the temperature up to optimum
increases the rate of reaction
o Increase in kinetic energy
o More successful collisions and formation
of ES complexes
 Increasing the temperature above the
optimum decreases the rate of reaction
o As temperature increases, hydrogen and
ionic bonds in the active site begin to
break
o Change in tertiary structure leads to
denaturation
 Rate of reaction is 0 when all enzymes have
denatured
EFFECT OF pH
 Enzymes have optimum pH where rate of
reaction is highest
 At pH above and below optimum pH, rate of
reaction decreases
o Change in pH alters charges on amino
acids of the active site, substrate cannot
attach to active site
o Causes hydrogen and ionic bonds in
active site to break
o Change in tertiary structure leads to
denaturation
 Substrate cannot bind to active site and form
ES complex
 Fewer ES collisions and formation of ES
complexes
o Not enough substrate to fill active sites
so further addition of enzyme molecules
has no effect on rate

EFFECT OF ENZYME CONCENTRATION
 Increasing enzyme concentration increases
rate of reaction
o More active sites available to form ES
complexes to increase rate of reaction
 When enzyme concentration exceeds
substrate concentration, rate of reaction
plateaus
o Not enough substrate to fill active sites
so further addition of enzyme molecules
has no effect on rate
COMPETITIVE INHIBITORS
Competitive inhibitors decrease the rate of
reaction
 They have a similar shape to the substrate
 Blocks/competes with substrate for active
site so substrate cannot bind
 Fewer ES complexes can form
Increasing the concentration of substrate can
reduce the effect of the competitive inhibitor
 Competitive inhibition is reversible so
substrate is able to bind at higher
concentrations
NON-COMPETITIVE INHIBITORS
Non-competitive inhibitors also decrease the
rate of reaction but are irreversible.
 Non-competitive inhibitors bind to a site
away from the active site – allosteric site
 This changes the tertiary structure and thus
the active site of the enzyme
 Substrate is no longer able to bind to the
active site so fewer ES complexes form
 Increasing substrate concentration has no
effect on the rate of reaction as the active
site is permanently changed

EFFECT OF SUBSTRATE CONCENTRATION

 Increasing substrate concentration
increases rate of reaction
o More substrate molecules available to
occupy active sites
o More successful ES collision and
formation of ES complexes
 When substrate concentrations exceeds
enzyme concentration, rate of reaction
plateaus
o All active sites are saturated as there is
excess substrate so not enough active
sites available to increase rate
 1.5.1 Nucleic acids: Structure of RNA and DNA
NUCLEOTIDE STRUCTURE
Individual nucleotides are made up of three
components:
 A pentose sugar
 A phosphate group
 A nitrogenous base
o Cytosine, adenine, guanine, thymine or
uracil
These components are joined by condensation
reactions to form a mononucleotide.
 Two mononucleotides can be joined in a
condensation reaction by a phosphodiester
bond to form a dinucleotide
 Continuous linking of these mononucleotides
forms a polynucleotide
RNA STRUCTURE
RNA is a polymer made up of ribonucleotides.
 It has a singular relatively short chain
 The pentose sugar is always ribose
 Includes cytosine, guanine, adenine and
uracil
tRNA transfers genetic information from DNA to
the ribosomes.
rRNA makes up ribosomes, alongside other
proteins.
mRNA is involved in protein synthesis.
DNA STRUCTURE
DNA is a polymer made up of
deoxyribonucleotides.
 It is made up of two long strands of
nucleotides
o These strands are joined by hydrogen
bonds between complementary bases
o These strands are antiparallel and twist
into a double helix
 The pentose sugar is always deoxyribose
 It contains adenine, thymine, cytosine and
guanine
BASE PAIRING
In DNA, the two strands are held together by
hydrogen bonds between complementary bases:
 Adenine is complementary to thymine
 Guanine is complementary to cytosine
The quantities of adenine and thymine are always
the same, as well as the quantities of cytosine
and guanine.
However, the ratio of adenine and thymine to
cytosine and guanine varies between species.
RNA VS DNA
Similarities:
 Both RNA and DNA nucleotides contain a
pentose sugar, nitrogenous base and
phosphate
 Both RNA and DNA nucleotides are joined by
condensation reactions to form
phosphodiester bonds
 Both nucleotides posses four nitrogenous
bases
Differences:
 DNA nucleotides have deoxyribose sugar,
whereas RNA nucleotides have ribose sugar
 DNA nucleotides can have thymine, whereas
RNA nucleotides have uracil instead
 DNA molecules are double stranded,
whereas RNA molecules are single stranded
 DNA is longer whereas RNA is shorter
STRUCTURE RELATED TO FUNCTION
DNA is double stranded
 Both strands can act as template for semi-
conservative replication
Weak hydrogen bonds between bases
 Can easily be broken for replication and
protein synthesis
Many hydrogen bonds between bases
 Provides stability to DNA
Double helix with sugar phosphate backbone
 Protects from outside chemical and physical
forces
Double helix
 DNA is coiled and compact
Base pairing
 Leads to DNA being able to replicate and
transfer information as mRNA
 1.5.2 Nucleic acids: DNA replication
suspended in a solution in separate tubes
SEMI-CONSERVATIVE REPLICATION and spun in a centrifuge

For semi-conservative replication to take place

there are four requirements:
 The four types of nucleotide, each with their
bases
 Both strands of the DNA molecule act as a
template for the attachment of these
nucleotides
 DNA polymerase
 A source of chemical energy is required to
drive the process
The process of semi-conservative replication is
as follows:
 DNA helicase breaks the hydrogen bonds
linking the base pairs of DNA
 Double helix separates into its two strands
and unwinds
 Each strand acts as a template to which
complementary free nucleotides binds by Before DNA replication:
complementary base pairing  DNA of bacteria contained only N15 so had
 Nucleotides are then joined in a two heavy (original) strands
condensation reaction by DNA polymerase After 1 round of DNA replication:
to form a new DNA molecule  DNA of bacteria grown originally in N15
 New DNA molecule contains half the original nutrient solution was then transferred for
DNA – semi-conservative replication one division to a solution containing N14
o DNA molecules contained 1 heavy
DNA POLYMERASE (original) and 1 light strand
DNA polymerase has a specific shaped active After 2 rounds of DNA replication:
site which only binds to a complementary  Another division of 1 heavy and 1 light
substrate stranded DNA
 DNA polymerase can only bind to and add o 50% of DNA molecules contain 1 heavy
nucleotides at the phosphate (3’) end (original) and 1 light strand, 50% contain
 It works from 5’ to 3’ both light strands

EVIDENCE FOR SEMI-CONSERVATIVE

REPLICATION
Meselson and Stahl conducted an experiment to
show that DNA replication is semi-conservative:
 Bacteria were grown in a nutrient solution
containing heavy nitrogen (N15) for several
generations
o N15 was able to be incorporated into the
bacterial DNA bases
 They were then transferred to a nutrient
solution containing light nitrogen (N14) and
allowed to grown and divide twice
 During this process, DNA from different
samples of bacteria was extracted,
 1.6 ATP
STRUCTURE OF ATP
ATP is a phosphorylated macromolecule which
contains:
 Adenine – nitrogenous base
 Ribose – 5-carbon sugar that acts as a
backbone
 Phosphates – chain of three phosphate
groups
HOW DOES ATP STORE ENERGY
ATP HYDROLYSIS
The three phosphate groups are key as to how
ATP stores energy.
 The bonds between each phosphate group is
unstable so have a low activation energy
o This means they are easily broken
 When these bonds break, they release a
considerable amount of energy
ATP hydrolysis is catalysed by ATP hydrolase
ATP  ADP + Pi
ATP CONDENSATION
The conversion of ATP to ADP is a reversible
reaction, but requires the addition of an inorganic
phosphate to ADP to reform ATP:
ADP + Pi  ATP
This is catalysed by ATP synthase.
The addition of a phosphate to ADP to reform ATP
can occur in three ways:
 Photophosphorylation
 Oxidative phosphorylation
 Substrate-level phosphorylation
PROPERTIES OF ATP
ATP cannot be stored – it is an immediate source
of energy
 The low activation energy of the phosphate
bonds means they are unstable and thus
release energy immediately
As such, ATP is a better immediate source of
energy than glucose as:
 Each ATP molecule releases less energy
than each glucose molecule
o It releases energy in smaller more
manageable quantities
 The hydrolysis of ATP to ADP is a one-step
reaction that releases immediate energy
o Glucose breakdown is a series of steps
which releases energy slower
ROLES OF ATP
ATP is used in energy-requiring processes in
cells including:
 Metabolic processes
o ATP provides the energy needed to build
up macromolecules from their basic
units
 Movement
o ATP provides the energy for muscle
contraction
 Active transport
o ATP provides energy to change the shape
of carrier proteins in plasma membranes
o This allows molecules or ions to be
moved against a concentration gradient
 Secretion
o ATP is needed to form the lysosomes
necessary for the secretion of cell
products
 Activation of molecules.
o The inorganic phosphate released during
the hydrolysis of ATP can be used to
phosphorylate other compounds
o This makes them more reactive, thus
lowering the activation energy in
enzyme-catalysed reactions
 1.7 Water and Inorganic ions
HYDROGEN BONDING
Water is a polar molecule
 Oxygen atom has a partial negative charge
 Hydrogen atom has a partial positive charge
Partial negative charge on oxygen attracts
slightly positive charge on hydrogen of other
water molecules.
This forms hydrogen bonds between the
hydrogen of one water molecule and the oxygen
of another water molecule.
PROPERTIES OF WATER
Water has several properties that are important
in biology.
HIGH SPECIFIC HEAT CAPACITY
Water is polar meaning many hydrogen bonds
form between water molecules.
 This allows water to absorb relatively large
amounts of heat energy before its
temperature changes
Therefore, it has a high specific heat capacity.
Water can therefore act as a buffer against
sudden temperature changes
 This helps maintain a stable internal body
temperature for organisms, since they are
mostly water
HIGH LATENT HEAT OF VAPORISATION
Water is polar so many hydrogen bonds form
between water molecules.
 These can absorb a lot of energy before
breaking, when water evaporates into a gas.
Water therefore gives a cooling effect upon
evaporation.
 This helps organisms maintain a constant
body temperature.
COHESION
Water is polar so many hydrogen bonds form
between water molecules.
 This means water molecules tend to stick
together
Water therefore has high cohesive forces which
can support columns of water (e.g. in xylem) and
provides surface tension at the water-air
boundary
SOLVENT
Water is polar so many hydrogen bonds form
between water molecules.
 This means it can separate ionic compounds
since the positive ions are attracted to the
partially negative oxygen and the negative
ions are attracted to the partially positive
hydrogen
Water can therefore dissolve other substances
(e.g. inorganic ions, enzymes, urea etc.)
 It acts as a medium for metabolic reactions
 It acts as a transport medium (e.g. in xylem)
METABOLITE
Water is also a reactive compound.
 Condensation reactions release water and
forms a chemical bond
 Hydrolysis reactions require water to break
a bond
INORGANIC IONS
Inorganic ions occur in solution in the cytoplasm
and body fluids of organisms, in high
concentrations in some and low concentrations
in others.
PHOSPHATE (PO43-):
 Structural role in DNA
o Give stability in the sugar-phosphate
backbone
 Stores energy in ATP
HYDROGEN (H+):
 Determine the pH of solutions and therefore
functioning of enzymes
SODIUM (Na+):
 Co-transport mechanism for glucose/amino
acids across plasma membranes
 Involved in generating nerve impulses and
muscle contraction
IRON (Fe2+):
 Component of haemoglobin contained in red
blood cells
 Transports oxygen around the body – oxygen
temporarily binds to it, so it becomes Fe3+