CHEMISTRY OF LIFE

Vocabulary
• tertiary structure
• protein, peptide, hydrolyse, hydrolysis, helix, helices,
enzyme, inhibition, inhibitor
• the shape / tertiary structure of proteins is caused by ...
• the forces involved are...
• the effect of these interactions is to ...
 Learning Objectives
• know that proteins are polymers and be able to describe sequences in relation to properties
• be able to determine the structure of a protein from hydrolysis data
• distinguish between primary, secondary and tertiary protein structures and explain the occurrence of alpha
helices and beta-pleated sheets
• know the tertiary protein structure and recognise the forces which govern its shape
• understand the process of enzyme catalysis and the specific action of enzymes in terms of a „lock and key‟
model
• recognise and understand competitive inhibition
• understand denaturation and how it can be brought about
• know and understand a simple model of the structure of DNA including hydrogen bonding between base
pairs
• explain DNA encoding in outline for the amino acid sequence of proteins
• explain the chemistry of DNA mutation from provided data
• discuss the genetic basis of disease in terms of altered base sequence, causing alterations in protein
structure and function
• explain how modification to protein/enzyme primary structure can result in new structure and/or function
• describe using block diagrams the structure and hydrolysis of ATP and how this provides a source of
energy
• know and describe simply the role of specified metals which are essential to life
• know some sources of heavy metal pollution in the environment and how these metals enter the food chain
• recognise that some metals are very toxic and be able to describe simply their effects on proteins
Proteins
FAQ
• https://www.youtube.com/watch?v=2Jgb_DpaQhM
• http://www.biology-questions-and-answers.com/protein-
structure.html
Proteins
• The amino acid monomers are linked by peptide bonds to
form the polypeptide chain.
• An amino acid unit within a polypeptide chain is called an
“amino acid residue”
• Each protein has a unique sequence of amino acid
residues determined by DNA.
• Hemoglobin in red blood cells, responsible for transporting
oxygen, has a formula of C2952H4664O832N812S8Fe4 and a
molecular mass of about 65000.
• Collagen, the major structural protein in our bodies, is
made of three polypeptide chains, each around 1000
amino acids long, coiled round each other in a triple helix.
The Amino Acid Abbreviations
Polypeptide - Protein
Protein Sequence
The Structure of Proteins
• Primary structure: This is the sequence of amino acids in a
polypeptide chain, and is the direct result of the coding
sequence in the gene.
• Secondary structure: This is the regular structural
arrangements of the polypeptide chain that result from
hydrogen bonding between peptide bond regions of the chain.
• Tertiary structure: This is the overall folding of a polypeptide
chain that is the result of interactions between the amino acid
side-chains.
• Quaternary structure: The three-dimensional structure of a
multi-subunit protein and how the subunits fit together. In this
context, the quaternary structure is stabilized by the same non-
covalent interactions and disulfide bonds as the tertiary
structure.
 14

Primary Structure
 Each polypeptide chain is a linear polymer of amino
acids and as such has an amino- (or N-)terminal end
and a carboxy- (or C-)terminal end.

 Each polypeptide therefore has ‘direction’ (from N to C)

and the sequence of amino acid residues in a chain is
known as the primary structure of the polypeptide.

 The primary structure of a polypeptide chain is

genetically controlled and is crucial in determining the
other levels of structure that the protein can adopt.
 15

 The primary structure of the insulin A chain is shown

below.
 16

 In the cell, a polypeptide chain is always synthesized from

the N-terminal end to the C-terminal end.
 Thus, when writing out the primary sequence of a
polypeptide chain the amino acids are numbered from the
N-terminal end.
 The positions of any cysteine residues will determine the
possible formation of disulfide bridges to stabilize the 3D-
tertiary structure of the protein.
 17

Secondary Structure
• Each polypeptide has a „backbone‟ that runs the length of
the chain.
• As the only difference between the different amino acids
lies in their R-groups, this backbone is essentially the
same for all protein chains [ –C–C–N–C–C–N– etc. ].
• This polypeptide backbone is flexible and in certain
regions of the protein can fold in a regular manner, known
as secondary structure.
 18

 These structures are stabilized by

hydrogen bonding between the
peptide bond regions of the chain’s
backbone.

 The N–H of one peptide link

hydrogen bonding to the C=O
of another.
 19

• This type of folding, stabilized by the intramolecular

hydrogen bonding, gives rise to certain structural features
which are found in many different types of protein.
• Two of the most stable arrangements at this level of
protein folding are the ɑ-helix and the β-pleated sheet.
• In the ɑ-helix the H-bonds are formed with every 4th
amino acid residue, resulting in the backbone spiraling to
form a rod-like structure.
 20

Secondary Structure

-helix as found in Keratin

 21

Secondary Structure

 In the -pleated sheet structure, H-bonds are formed

between 2 polypeptide chains or between completely
different areas of the same chain.

-pleated sheet as found in

silk fibroin
 22

Secondary Structure
• Regions of regular secondary structure occur in many
proteins.
• This structure has distinct ɑ-helical regions, represented
by the „cylindrical rods‟, and β-pleated sheet regions,
represented by the „arrows‟.
 23

Tertiary Structure
• A series of possible interactions between the R-
groups of the different amino acid residues in a
protein chain produces a third level in the
hierarchy of protein folding.
• This is known as tertiary structure and is crucially
important to a protein‟s function.
• The three-dimensional shape or conformation of
a protein chain is maintained by a series of
mainly non-covalent, intramolecular interactions
between the R-groups of the amino acids making
the chain.
 24

These interactions include:

• van der Waals (instantaneous dipole-induced

dipole) forces between non-polar side-chains
• hydrogen bonding between polar R-groups,
• ionic bonds (salt bridges) between ionized R-
groups,
• covalent disulfide bridges formed between
cysteine residues at different locations in the
primary sequence
 25

Three of the important tertiary structure interactions

are shown below:
a – ionic bonds ; b – hydrogen-bonding ; c – disulfide bridges
 26

The nature of
the interactions
responsible for
protein tertiary
structure.
 27

• A fourth level of
protein structure is
called the quaternary
structure, as shown in
the bottom figure.

• It is characterized by
proteins with two or
more separate
polypeptide chains.
Hydrolysis of Proteins
Hydrolysis of Proteins
The slow way
• The protein is heated with 6 M hydrochloric acid for about 24 hours at
110°C. (6M hydrochloric acid is slightly more than semi-concentrated.)

The fast way

1. Protein samples are placed in tubes in a sealed container containing

6 M hydrochloric acid in an atmosphere of nitrogen.
2. The whole container is then placed in a microwave oven for about 5 -
30 minutes (depending on the protein) with temperatures up to 200°C.
3. The hydrochloric acid vaporises, comes into contact with the protein
samples and hydrolyses them.

• This method is used to hydrolyse small samples of protein during protein

analysis.
Analysis of Hydrolysis
• After hydrolysis of an unknown tripeptide the following
amino acids were found: Ala, Cys, Ile.
• What are the possible tripeptides?
Task

What was the original peptide?

Answer
Task
Determine the sequence of hexapeptide based on the
following data.

• Amino acid composition: (2 Arg, Ala, Ser, Val,Tyr)

• N-terminal analysis of the hexapeptide: Ala
• Carboxypeptidase digestion: No digestion (At C-terminal
no aromatic or branched hydrocarbon chains or positively
charged amino acids (arginine, lysine)).

• Trypsin digestion: (Arg,Ala,Val) and (Arg,Ser,Tyr)

• Chymotrypsin digestion: (Ala,Arg,Val,Tyr) and (Arg,Ser)
Nice to know, maybe
Answer
• Ala-Val-Arg-Tyr-Arg-Ser
Enzymes
• https://www.youtube.com/watch?v=ok9esggzN18
 38

 Enzymes are nature’s catalysts and are large protein

molecules

 In common with other catalysts, enzymes provide

an alternative reaction pathway that has a lower
activation energy barrier than the uncatalysed
reaction.

 Enzymes are very effective catalysts, despite many

being restricted to operating under very mild
conditions.
 39

 Enzymes are very specific, generally catalysing only one

particular reaction. Carbonic anhydrase, for instance, is
an enzyme in red blood cells that catalyses the reaction:
CO2 + H2O → H2CO3

 This enzyme increases the rate of this reaction up to a

million fold, increasing the efficiency of removal of
carbon dioxide from our bloodstream.

 Each enzyme has a specific substrate; the substrate is

the target molecule acted upon during the enzyme-
catalysed reaction.
 40

Enzymes differ from ordinary chemical catalysts in several

important respects:

 Higher reaction rates – the rates of enzyme catalyzed

reactions are typically increased by factors of 106 to 1012
times compared to the uncatalyzed reaction and are
several orders of magnitude greater than those of the
corresponding chemically catalyzed reaction.

 Milder conditions – enzyme catalyzed reactions

occur at temperatures below 100 °C, atmospheric
pressure, and at pH’s around neutrality.
 41

Enzymes differ from ordinary chemical catalysts in several

important respects:

 Greater reaction specificity – enzymes are much more

choosy with regard to their substrate and products:
enzyme-catalyzed reactions are ‘clean’, that is they do not
produce side products.

 Capacity for regulation – the catalytic activities of many

enzymes can be varied by the concentrations of
substances other than the substrate (non-competitive
inhibition – discussed later).
Enzyme activity is the number of moles of substrate
turned to product per minute and the turnover number is
the number of substrate molecules reacted per enzyme per
minute.

Enzyme turnover number

carbonic anhydrase 36 000 000

catalase 5 600 000

comparison of
β-amylase 1 100 000 the catalytic
β-galactosidase 12 500 efficiency of
certain enzymes
phosphoglucose isomerase 1 240

succinate dehydrogenase 1 150

42
 43

The Active Site

 The complicated folding of the protein chain to form the
tertiary structure of an enzyme gives rise to ‘pockets’ of
precise geometric shape on the surface of the enzyme.

 The precise shapes of these pockets have evolved to

‘recognize’ and hold in place a particular substrate
molecule while it reacts.

 Because this region is where the enzyme-catalysed

reaction takes place it is known as the active site of
the enzyme.
 44

 The active site usually occupies less than 5% of an

enzyme’s surface area and involves only a small number
(3 to 12) of specific amino acids which side chains form
weak bonds with the substrate.

 The rest of the enzyme structure maintains and

protects the shape of the active site.
 Lysozyme is a water-soluble enzyme present in
tears and nasal mucus. It has an important role in
protecting us from bacteria because it breaks
down the carbohydrates present in the bacterial
cell wall. (diagram next slide)
 45

The enzyme lysozyme, with the carbohydrate substrate

lying in the active site.
 46

The Lock and Key Model

 The precise specificity shown by enzymes led to
Fischer (in 1894) proposing a model of enzyme
activity often referred to as the ‘lock and key’
mechanism.

 He suggested that enzymes catalysed

reactions by binding to substrates in a
manner similar to how a key (the substrate)
fits into a lock (the enzyme).
 47

The Lock and Key Model

Only one substrate will fit into the active site,
just as only one key fits a lock.
 48

The energy profile shown below illustrates how the formation

of the enzyme-substrate complex reduces the energy
requirement for the reaction to proceed:
 49

The overall reaction between enzyme and its substrate

can be represented by the following equation:

ENZYME + SUBSTRATE

(lock) (key)

⇌
ENZYME-SUBSTRATE
(key in lock)
→

ENZYME + PRODUCTS
 50

 The first stage of the reaction is reversible, since the

activation energy for the dissociation of the E–S
complex back to E + S is similar in size to that for
the breakdown of E – S into E + P.

 Once the products have been formed, they leave

the active site of the enzyme.

 The enzyme is then free to combine with a new

substrate molecule.
 51

The Lock and Key Model

Lysozyme catalyzes the hydrolysis of polysaccharides in the cell
walls of bacteria as follows:

Lysozyme

Polysaccharide
Lysozyme – Polysaccharide

Hydrolyzed product
Cofactors
• Many enzymes need a non-protein group in order to
function as catalysts.
• There are two types of cofactors:
• Prosthetic group – ions or molecules permanently
bound to the enzyme
• Coenzyme – complex molecules, often synthesised
from vitamins, bind temporarily to the active site of the
enzyme (co-substrate)
 53

Competitive Inhibition
 Competitive inhibitors of a particular enzyme
are molecules that have a similar shape to the
substrate molecule.

 Such molecules can bind to the active site but

cannot participate in the catalyzed reaction.

 When they are present in the active site no

reaction is taking place and the correct substrate
cannot attach to the enzyme.
 This type of inhibition is reversible by an
increase in substrate concentration.
 54

A Model of Competitive Inhibition is shown below:

 55

An example of competitive inhibition is the inhibition

of succinate dehydrogenase by malonate which
structurally resembles the substrate, succinate:

Adding more
of the
succinate will
help to
increase the
enzyme activity.
 56

Non-Competitive Inhibition
 Molecules can bind on to regions of the enzyme
other than the active site and still affect enzyme
activity.

 This is known as non-competitive inhibition.

 In non-competitive inhibition the inhibitor again

binds to the enzyme, preventing the catalysed
reaction from occurring.
 However, in this case, the inhibitor does not bind
to the active site. Instead it binds to another
position on the enzyme.
 57

Non-Competitive Inhibition
 This binding is thought to cause one of the
following:
• The active site to change shape so that the
substrate cannot bind.

• The enzyme-substrate complex to change shape so

that the reaction cannot take place.

 The inhibitor is not shaped like the substrate and

there is no competition between the substrate
and the inhibitor. Therefore, the inhibition cannot
be overcome simply by adding more substrate.
 58

A model for non-competitive inhibition

 59

Non-Competitive Inhibition
 This type of inhibition is reversible and can provide an
important mechanism for feedback control of a
metabolic pathway in cells.
 One example involves the effect of heavy metal ions,
such as silver or mercury, on a range of enzymes.

 Such enzymes contain amino acid side-chains that

contain –SH groups.

 As shown in the figure on the next slide the Ag+ or

Hg+ reversibly replaces the H atom on one or more
–SH groups.
 60

Non-Competitive Inhibition

 The resulting modification does not allow disulfide bridges

to form, and so changes the shape of the enzyme
sufficiently enough to prevent the catalyzed reaction taking
place.
 61

Factors affecting Enzyme Activity

 Recognition and molecular ‘fit’ are the key ideas
behind enzyme function.

 Even subtle changes in pH or temperature can

modify the interactions involved in molecular
shape and recognition, resulting in an enzyme
working at less than maximum efficiency.

 Interactions with other chemical substances that

cause irreversible changes in structure can
also result in the destruction of enzyme activity
known as denaturation.
 62

Temperature
A profile of enzyme
activity vs Temperature

When T increases between 0 °C to ~40 °C the rate

of enzyme activity increases because:
• collision frequency increases.
• more collisions with energy greater than Ea.
 63

Temperature
 For most enzymes the rate of reaction starts to
decrease above 40 °C.

 Above this temperature increased thermal motion

of the polypeptide chain and the enzyme starts to
lose its tertiary structure.

 The enzyme molecules are progressively

denatured, causing the shape of the active site to
change.
 Above 65 °C the enzymes from most organisms are
completely denatured (lost its tertiary structure).
 64

pH
 Extremes of pH (high acidity or alkalinity) will
denature proteins.
 Even small changes around neutral pH can affect
the ionization of amino acid side-chains in the
active site and/or the substrate itself:
 65

pH
If enzyme activity depends on particular residues in the
active site being charged or not, then a shift of just one
pH unit can change the enzyme activity significantly.

Curves showing
optimal pH for
selected digestive
enzymes
 66

pH
The explanations for this figure are as follows:
 Pepsin hydrolyses proteins to peptides in the
very acidic conditions of the stomach.

 Amylase, found in saliva, hydrolyses starch to a

mixture of glucose and maltose. The pH of saliva
is approximately neutral.

 Trypsin hydrolyses peptides to amino acids in the

mildly alkaline conditions of the small intestine.
Chemical denaturing
• If enzymes are exposed to extremes of pH or high
temperatures the shape of their active site may change.
• If this happens then the substrate will no longer fit into the
enzymes. This means the key will no longer fit the lock. We say
that the enzyme has been denatured.
• High salt concentration changes the ionic environment of
an enzyme, disrupting ionic interactions between different
regions of the chain.
• Urea denatures proteins by disrupting the hydrogen bonds
that maintain the secondary and tertiary structure of
proteins.
DNA
DNA Videos
• https://www.youtube.com/watch?v=NNASRkIU5Fw
• https://www.youtube.com/watch?v=q6PP-
C4udkA&ebc=ANyPxKqdHl-
Ydva4SyJNq3aVt1Ys_QyGCo0tpAL2flpwI0tzk4AqvzQqLv
Yk36RwReRl-83Owh4kf7iXkO_3IddkBKZM6J-Ddg
 70

Nucleic Acids
Nucleic acids play an essential role in the origins of life,
evolutionary development, and the transfer of
genetic information from one generation to another.

Deoxyribonucleic acid (DNA) controls heredity

information on a molecular level:

 It is a self-replicating molecule capable of passing

genetic information from one generation to the next.

 It contains in its base sequence the genetic code

used to synthesize proteins.
 71

Nucleic Acids
A strand of DNA is a macromolecule made by the
condensation polymerization of units called nucleotides.

a phosphate group

a nitrogen-containing
organic base

a sugar (deoxyribose – a
pentose sugar with a five
member ring)
The three components that make up a nucleotide.
Nucleic Acid - NA
• Nitrogenous bases
 73

Nucleic Acids
The phosphate group is attached by an ester link to the
deoxyribose.

The final components of the nucleotides in DNA are the

four different bases:

 Adenine (A)
planar two-ring structures (purines)

 Guanine (G)

 Thymine (T) planar single-ring molecules (pyrimidines)

 Cytosine (C)
 74

Nucleic Acids
The DNA double helix

The strands are linked

together by hydrogen
bonding between the
bases as shown:
 76

The DNA double helix

 These two anti-parallel strands are twisted together in a
double helix with the bases on the inside and the sugar-
phosphate backbones on the outside.

 The bases positioned between the two chains lie at right

angles to the backbone, filling the space between the
strands.

 Two hydrogen bonds form between each adenine-thymine

pair (A = T). Three hydrogen bonds are formed between
a guanine-cytosine pair (G≡C).
 77

The DNA double helix

The bases always pair up as follows:

 adenine is always paired with thymine; two hydrogen

bonds
 guanine is always paired with cytosine; three hydrogen
bonds
 This is known as complementary base pairing and is key
to the transfer of the information stored in the sequence
of the bases along the DNA chains

The structure of DNA is kept stable by:

 Hydrogen bonding and van der Waals’ forces between

the stacks of bases
 78

Nucleic Acids
The DNA double helix
The Genetic Code
• Three base sequence = 1 codon = 1 amino acid

For example:
• GCG = Alanine
• GGC = Glycine

• AUG = start codon

• UAA, UAG, UGA = stop codon
From DNA to Protein
From DNA to Protein
• The code from DNA is first transcribed ("copied“)
to a messenger RNA (mRNA).
• the RNA copied from the DNA gene sequence for a
particular polypeptide chain. The „message‟ encoded in
the mRNA molecule is translated into the primary
sequence of a polypeptide chain.

• In RNA the important base pairs are:

• adenine (A) pairs with uracil (U);
• guanine (G) pairs with cytosine (C).
• Individual amino acids won't interact with the messenger
RNA chain.
• The amino acids have to be carried to the messenger
RNA by another type of RNA known as transfer RNA
(tRNA).
• Transfer RNA (tRNA) is responsible for carrying amino acids to the
messenger RNA and then holding them there in a way that enables
them to join together.

• All of this is controlled by a ribosome - a hugely

complicated structure involving protein molecules and yet
another form of RNA (ribosomal RNA or rRNA).
• The transfer RNA carrying a methionine attaches itself to
the start codon by pairing its anti-codon bases with the
complementary bases on the messenger RNA.
• Next another transfer RNA molecule with its attached
amino acid binds to the next codon along the chain.
• At the same time a peptide bond is made between the two
amino acids.
• Eventually, the ribosome will come to a stop codon. The
stop codons don't code for any amino acids, and so the
process comes to a halt.
• The protein chain produced up to that point is then
released from the ribosome, and then folds itself up into
its secondary and tertiary structures.
Protein synthesis
• https://www.youtube.com/watch?v=x5ZXQo-xeMo
 87

Genetic Mutations
 A mutation is a change in the intended DNA sequence.

 Rare copying errors when DNA replicates or is

transcribed into RNA can cause changes in the
sequence of bases which makes up the genetic code.

 Radiation and some chemicals can also cause changes.

 A couple of examples of this are shown later in the

following slides.
Types of mutation
Substitution: A substitution is a mutation that exchanges
one base for another.

Such a substitution could:

• change a codon to one that encodes a different amino
acid and cause a small change in the protein produced.
• change a codon to one that encodes the same amino acid
and causes no change in the protein produced. These are
called silent mutations.
• change an amino-acid-coding codon to a single "stop"
codon and cause an incomplete protein. This can have
serious effects since the incomplete protein probably
won't function.
Types of Mutation
Insertion
• Insertions are mutations in which extra base pairs are
inserted into a new place in the DNA.

Deletion
• Deletions are mutations in which a section of DNA is lost,
or deleted.
 90

Sickle cell anemia

 People with sickle cell anemia have sickle

hemoglobin (HbS) which is different from the
normal hemoglobin (HbA).

 The red blood cells of these patients do not have

the normal disc shape, but have a crescent moon
(or sickle) shape.

 The result of the mutation is an abnormal amino

acid sequence in one of the protein chains in
hemoglobin (the β-chain).
 91

Sickle cell anemia

The abnormality mentioned alters a single amino acid at

the sixth position of the 146 amino acid chain:

Normal β-chain Val His Leu Thr Pro Glu Glu

Sickle cell β-chain Val His Leu Thr Pro Val Glu
 92

Sickle cell anemia

 Because of their shape, sickle-shaped red blood

cells cannot squeeze through small blood vessels
as easily as the almost doughnut-shaped normal
cells.
 This can lead to these small blood vessels getting
blocked, stopping oxygen from getting through to
where it is needed.

 This can then lead to severe pain and damage to

organs in the body.
 93

Cystic Fibrosis

 Cystic fibrosis is a relatively common genetic disorder.

 The condition affects the lungs, pancreas, gut and

sweat glands.

 Instead of the normal fluid secretions, a thick sticky

mucus forms.

 This viscous mucus blocks and damages the intestines

and lungs.
 94

Cystic Fibrosis

 Cystic fibrosis affects the cells that line the cavities and
tubes inside organs such as the lungs.

 The CFTR membrane protein in these cells creates a

channel for chloride ions to diffuse out of the cell.

 In a person with cystic fibrosis the CFTR protein does

not work properly, due to a mutation in the gene.

 The chloride ion concentration in the cell builds up

causing water to move into the cell by osmosis. As a
result the mucus covering the cells lining the airways
becomes thick and sticky.
 95

Cystic Fibrosis
 Hundreds of different mutations have been identified
that can give rise to the disease.

 The most common mutation is the deletion of three

nucleotides on chromosome 7 which result in the loss
of the 508th amino acid in the structure of the
protein.
 96

Cystic Fibrosis
 97

Hemophilia
 Hemophilia is a genetic disorder whereby there is a
lack of the protein used to clot blood.

 This means that if someone with hemophilia cuts

themselves, the wound will just continue to bleed.

 One of the many mutations which cause this disease

results from changing a single base at the beginning of
a codon for arginine (CGA) somewhere in the gene to
give UGA.
 What amino acid is formed from the codon UGA and
why is this a problem?
ATP - Energy Transfer in
Biochemical Reactions
 99
Energy Transfer in Biochemical Reactions

Living things require a continuous supply of energy for:

 Muscle contractions

 The transport of molecules and ions in and out of

cells, through their membranes.

 The synthesis of molecules such as proteins,

starch, fats, vitamins and coenzymes.
Adenosine Triphosphate (ATP)

 This nucleotide has a crucial role to play in

making energy available for metabolic reactions in
all living organisms.

 ATP is the short term energy source for cellular

activity.

 In animal cells this nucleotide is synthesized in the

mitochondria of the cell.
Adenosine Triphosphate (ATP)
ATP
 104

Adenosine Triphosphate (ATP)

The hydrolysis of ATP is an exothermic reaction as

follows:
ATP + H2O ⇌ ADP + Pi ΔH = –30 kJ mol–1

 The release of the end phosphate group is favored

by the repulsion between the negatively charged
O atoms on the adjacent phosphate groups.
ATP Hydrolysis Mechanism
Hydrolysis of ATP
Enthalpy Changes in ATP
 108

Adenosine Triphosphate (ATP)

The role of ATP in metabolism.

Metals in Biological Systems
 110

Hemoglobin
Iron(II) ions (Fe2+) play
an integral role in the
structure and function of
hemoglobin.

 The water molecule which is bonded to

the bottom position in the diagram is
easily replaced by an oxygen molecule
(via a lone pair on one of the oxygens
in O2) - and this is how oxygen gets
carried in the blood by the hemoglobin.
 111

Zinc as an enzyme cofactor

Carbonic anhydrase removes CO2 from our blood,
increasing the rate of the following reaction 1 million
times:
CO2 + OH- → HCO3-

 Key to the activity of this enzyme is the zinc ion (Zn2+)

present in the active site of the enzyme.

 The high charge density of Zn2+ helps further ionize

H2O into H+ and OH-.

 Following release of the hydrogen carbonate ion a

further water molecule binds to the zinc and the
catalytic cycle begins again.
 112

Na+/K+ ion Transfer

Within living cells the Na+ ion concentration is lower, and
the K+ ion concentration higher, than the surrounding
liquid outside. The sodium potassium pump (NaK pump) is
vital to numerous bodily processes, such as nerve cell
signaling, heart contractions, and kidney functions.

 How this difference is achieved is important for all

cells, but particularly for nerve cells.
 When a nerve is stimulated Na+ ions pour into the
cell.
 In order to maintain ionic balance again the Na+ ions
have to be pumped out of the cells.
 113

Na+/K+ ion Transfer

ATP provides energy to make this ion pump operate.

 The pump is an active transport enzyme

called ATPase also known as the Na+/K+ pump.

 These enzymes are located in the cell

membranes.
 114

How the Na+/K+ pump works

 115

Water and Ion Channels

 116

Toxic Metals
 Heavy metals such as lead and mercury are toxic.
They interfere with the tertiary structure of proteins
and hence their effective function.

 The effects of these heavy metals are evident at

even relatively low concentrations.

 However, the problems associated with them are

made worse by the fact that these metals can be
concentrated within the food chain, as shown on the
next page.
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Toxic Metals

Bioaccumulation of mercury
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Toxic Metals
Mercury poisoning causes loss of muscle coordination
and mental functions and can enter the food chain by a
number of routes:
1. In waste water discharged into rivers from
factories that use mercury compounds in their
processes, such as mercury cathode cells used in
the production of sodium hydroxide
2. Mercury compounds have been used as fungicides
and these can be washed off crops into the soil.

3. Mercury compounds have been used to treat wood

and again they can be washed into rivers and
streams.
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Toxic Metals
Lead poisoning causes mental health problems and can
enter the environment as follows:

1. From drinking water in old water pipes made with

Pb.
2. Lead compounds form car exhausts can settle on
fruit and vegetables grown near roadsides and so
can get into the food chain in this way. Levels from
this form of pollution are falling as the use of lead-
free gasoline increases.
3. Lead compounds found in some paints can get into
the air.