Chapter 2

The Chemistry of
Life

2-1
Copyright (c) The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 The Chemistry of Life

• Atoms, Ions and Molecules

• Water and Mixtures
• Energy and Chemical Reactions
• Organic Compounds

2-2
 The Chemical Elements
• Element - simplest form of matter to have
unique chemical properties
• Atomic number of an element - number of
protons in its nucleus
– periodic table
• elements arranged by atomic number
– 24 elements have biological role
• 6 elements = 98.5% of body weight
– oxygen, carbon, hydrogen, nitrogen, calcium, and phosphorus
• trace elements in minute amounts

2-3
2-4
 Atomic Structure
• Nucleus - center of atom
– protons: single + charge, mass = 1 amu (atomic
mass unit)
– neutrons: no charge, mass = 1 amu
– Atomic Mass of an element is approximately
equal to its total number of protons and neutrons

2-5
 Atomic Structure
• Electrons – in concentric clouds that surround the
nucleus
– electrons: single negative charge, very low mass
• determine the chemical properties of an atom
• the atom is electrically neutral because number of
electrons is equal to the number of protons
– valence electrons in the outermost shell
• determine chemical bonding properties of an atom

2-6
 Planetary Models of Elements
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Fourth
Third energy
Second energy level
First level
energy energy
level level

Carbon (C) 6p+, 6e-, 6n0 Nitrogen (N) 7p+, 7e-, 7n0 Sodium (Na) 11p+, 11e-, 12n0 Potassium (K) 19p+, 19e-, 20n0
Atomic number = 6 Atomic number = 7 Atomic number = 11 Atomic number = 19
Atomic mass = 12 Atomic mass = 14 Atomic mass = 23 Atomic mass = 39

p+ represents protons, no represents neutrons 2-7

 Ions and Ionization
• Ions – charged particles with unequal number
of protons and electrons

• Ionization -
transfer of
electrons from one
atom to another
( stability of 11 protons
Sodium
17 protons
Chlorine

valence shell)
12 neutrons 18 neutrons
atom (Na) atom (Cl)
11 electrons 17 electrons

1 Transfer of an electron from a sodium atom to a chlorine atom

Figure 2.4 (1) 2-8

 Anions and Cations
• Anion
– atom that gained electrons (net negative charge)
• Cation
– atom that lost an electron (net positive charge)
• Ions with opposite charges are attracted to each
other Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

+ –

Figure 2.4 (2)

11 protons 17 protons
Sodium Chloride
12 neutrons 18 neutrons
10 electrons ion (Na+) 18 electrons ion (Cl–)

Sodium chloride
2-9
2 The charged sodium ion (Na+) and chloride ion (Cl–) that result
 Electrolytes
• Salts that ionize in water and form solutions
capable of conducting an electric current.
• Electrolyte importance
– chemical reactivity
– osmotic effects (influence water movement)
– electrical effects on nerve and muscle tissue

• Electrolyte balance is one of the most important

considerations in patient care.
• Imbalances have ranging effects from muscle
cramps, brittle bones, to coma and cardiac arrest
2-10
2-11
Molecules and Chemical Bonds
• Molecules
– chemical particles composed of two or more
atoms united in a chemical bond

• Compounds
– molecules composed of two or more different
elements

• Molecular formula
– identifies constituent elements and shows how
many of each are present (e.g. H2O) 2-12
 Chemical Bonds
TABLE 2.3 Types of Chemical Bonds

• Chemical bonds –
forces that hold
molecules together, or
attract one molecule to
another
• Types of Chemical
Bonds
– Ionic bonds
– Covalent bonds
– Hydrogen bonds
2-13
 Ionic Bonds
• The attraction of a cation to an anion
• electron donated by one and received by the
other
• Relatively weak attraction that is easily
disrupted in water, as when salt dissolves

2-14
 Covalent Bonds
• Formed by sharing electrons
• Types of covalent bonds
– single - sharing of single pair electrons
– double - sharing of 2 pairs of electrons
– nonpolar covalent bond
• shared electrons spend approximately equal time
around each nucleus
• strongest of all bonds
– polar covalent bond
• if shared electrons spend more time orbiting one nucleus
than they do the other, they lend their negative charge to
the area they spend most time 2-15
 Single Covalent Bond

• One pair of electrons are shared

Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

p+ + p+ p+ p+

Hydrogen atom Hydrogen atom H H

Hydrogen molecule (H2)
(a)

Figure 2.6a 2-16

 Double covalent bonds:
Two pairs of electrons are shared each C=O bond
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Oxygen atom Carbon atom Oxygen atom

8p+ 6p+ 8p+

8n0 6n0 8n0

O C O
Carbon dioxide molecule (CO2)
(b) Figure 2.6b 2-17
 Nonpolar /Polar Covalent
Bonds
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Nonpolar covalent
C C C C bond
Electrons
shared
(a)
equally

O H
Polar covalent
O H bond
Electrons
shared
– + unequally
(b) Figure 2.7
2-18
 Hydrogen Bonds
• Hydrogen bond – a weak attraction between a
slightly positive hydrogen atom in one molecule
and a slightly negative oxygen or nitrogen atom
in another.
• Water molecules are weakly attracted to each
other by hydrogen bonds
• very important to physiology
– protein structure
– DNA structure

2-19
Hydrogen Bonding in Water
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

H
O

H
H

O
H O
H H
O
H
Covalent bond
H

Hydrogen bond
Figure 2.8

O
Water molecule
H H 2-20
 Water
• Water’s polar covalent bonds and its
V-shaped molecule gives water a set of
properties that account for its ability to
support life.
– solvency
– cohesion
– adhesion
– chemical reactivity
– thermal stability

2-21
 Solvency
• Solvency - ability to dissolve other chemicals
• water is called the Universal Solvent
– Hydrophilic – substances that dissolve in water
• molecules must be polarized or charged
– Hydrophobic - substances that do not dissolve in
water
• molecules are non-polar or neutral (fat)

• Virtually all metabolic reactions depend on the

solvency of water 2-22
 Water as a Solvent
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Oxygen
–

+ +

105°
(a)
Hydrogen

Na+ Cl –

(b)
Figure 2.9
• Polar water molecules overpower the ionic
bond in Na+ Cl-
– form hydration spheres around each ion
– water molecules: negative pole faces Na+, positive
pole faces Cl-
2-23
 Chemical Reactivity of Water
• is the ability to participate in chemical
reactions
– water ionizes into H+ and OH-

– water ionizes other chemicals (acids and

salts)

– water involved in hydrolysis and

dehydration synthesis reactions

2-24
 Thermal Stability of Water
• Water helps stabilize the internal temperature of
the body
– has high heat capacity – the amount of heat required to
raise the temperature of 1 g of a substance by 1 degree C.
• hydrogen bonds inhibit temperature increases by
inhibiting molecular motion
• water absorbs heat without changing temperature very
much

– effective coolant
• 1 ml of perspiration removes 500 calories (of heat)

2-25
 Solution, Colloid and Suspension

Solution Colloid Suspension

Figure 2.10 (2) 2-26

• Solution – consists of
particles of matter called the Solutions
solute mixed with a more
abundant substance (usually Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

water) called the solvent

• Solute can be gas, solid or
liquid
• Solutions are defined by the
following properties:
– solute particles under 1nm
– do not scatter light
– pass through most
membranes
(a) (b) (c) (d)
– will not separate on © Ken Saladin

standing Figure 2.10 (1)

2-27
• Most colloids in the body are
mixtures of protein and water
Colloids
• Many can change from liquid Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

to gel state
• Defined by the following
physical properties:
– particles range from 1 –
100 nm in size

– scatter light and are

usually cloudy

– particles too large to pass

through semipermeable
membrane (a) (b) (c) (d)
© Ken Saladin
2-28
– particles remain mixed Figure 2.10 (1)
 Suspensions and Emulsions
• Suspension Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

– defined by the following

physical properties
• particles exceed 100nm

• too large to penetrate

selectively permeable
membranes

• cloudy or opaque in
appearance

• separates on standing
(a) (b) (c) (d)
© Ken Saladin
2-29
• Emulsion Figure 2.10 (1)
2-30
 ***Acids, Bases and pH
• An acid is proton donor (releases H+ ions in
water)

• A base is proton acceptor (accepts H+ ions)

– releases OH- ions in water

• pH – a measure derived from the molarity of H+

– a pH of 7.0 is neutral pH (H + = OH-)
– a pH of less than 7 is acidic solution (H+ > OH-)
– a pH of greater than 7 is basic solution (OH- > H+ )

2-31
 pH
• pH - measurement of molarity of H+ [H+] on a logarithmic
scale
– pH = -log [H+] thus pH = -log [10-3] = 3

• a change of one number on the pH scale represents a 10

fold change in H+ concentration
– a solution with pH of 4.0 is 10 times as acidic as one with pH of 5.0

• Our body uses buffers to resist changes in pH

– slight pH disturbances can disrupt physiological functions and alter
drug actions
– pH of blood ranges from 7.35 to 7.45
– deviations from this range cause tremors, paralysis or even death

2-32
 pH Scale

Pure water Household

Bread, Milk, Household
(7.0) Egg white bleach
Wine, Bananas, black saliva
(9.5)
ammonia
(8.0)
Gastric juice vinegar tomatoes coffee (6.3 -–6.6) (10.5 - 11.0)
(2.4 -–3.5) (4.7) (5.0) Oven cleaner, lye
(0.9–3.0) Lemon
(13.4)
1M juice 1 M sodium
Hydrochloric (2.3) hydroxide
Acid (0) (14)

5 6 7 8 9
4 10
3 11
2 Neutral 12
Increa
1 y acidic singly
basic 13
ingl
Inc re a s

0 14

Figure 2.12
2-33
 Chemical Reaction
• chemical reaction – a process in which a
covalent or ionic bond is formed or broken
• chemical equation –symbolizes the
course of a chemical reaction
– reactants (on left)  products (on right)

• classes of chemical reactions

– decomposition reactions
– synthesis reactions
– exchange reactions 2-34
 Decomposition Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Reactions

• Large molecule breaks Starch molecule

down into two or more

smaller ones

• AB  A + B

Glucose molecules
Figure 2.13a 2-35
(a) Decomposition reaction
 Synthesis
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Reactions
Amino acids
• Two or more small
molecules combine to
form a larger one

• A + B  AB

Protein molecule
Figure 2.13b 2-36
(b) Synthesis reaction
 Exchange Reactions
• Two molecules exchange atoms or group of
atoms
• AB+CD  ABCD  AC + BD
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Stomach acid (HCl) AB + CD

C
D
A
B

and sodium
bicarbonate C A
(NaHCO3) from the D B

pancreas combine
to form NaCl and AC C A

H2CO3. +

Figure 2.13c BD D B
2-37
(c) Exchange reaction
 Reversible Reactions
• Can go in either direction under different
circumstances
• symbolized with double-headed arrow
• CO2 + H2O H2CO3 HCO3- + H+
– most common equation discussed in this book
– respiratory, urinary, and digestive physiology

• Law of mass action determines direction

– proceeds from the side of equation with greater quantity
of reactants to the side with the lesser quantity

• Equilibrium exists in reversible reactions when the ratio of

products to reactants is stable 2-38
 Reaction Rates
• Basis for chemical reactions is molecular motion and
collisions
– reactions occur when molecules collide with enough force and
the correct orientation
• Reaction Rates affected by:
– concentration: more reactants=faster rate
– temperature: higher temp=faster rate
– catalysts
• speed up reactions without permanent change to itself
• holds reactant molecules in correct orientation
• catalyst not permanently consumed or changed by the
reaction
• Enzymes – most important biological catalysts
2-39
 Organic Chemistry
• Study of compounds containing carbon

• 4 categories of carbon compounds

– carbohydrates
– lipids
– proteins
– nucleotides and nucleic acids

2-40
 Monomers and Polymers
• Macromolecules - very large organic
molecules
• proteins, DNA

• Polymers – molecules made of a repetitive

series of identical or similar subunits
(monomers)

2-41
 Polymerization
• joining monomers to form a polymer
• dehydration synthesis is how living cells form
polymers
– a hydroxyl (-OH) group is removed from one monomer,
and a hydrogen (H+) from another
• producing water as a by-product

• hydrolysis – opposite of dehydration synthesis

– a water molecule ionizes into –OH and H+
– the covalent bond linking one monomer to the other is
broken
– the –OH is added to one monomer
2-42
– the H+ is added to the other
 Dehydration Synthesis
• Monomers covalently bond together to form a
polymer with the removal of a water molecule
– A hydroxyl group is removed from one monomer and a
hydrogen from the next

Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Dimer

Monomer 1 Monomer 2

OH HO O

H+ + OH– H2O
(a) Dehydration synthesis

Figure 2.15a 2-43

 Hydrolysis
• Splitting a polymer (lysis) by the addition of a water
molecule (hydro)
– a covalent bond is broken

• All digestion reactions consist of hydrolysis reactions

Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Dimer

Monomer 1 Monomer 2

O OH HO
H2O H+ + OH–
(b) Hydrolysis

Figure 2.15b 2-44

 Organic Molecules:
Carbohydrates
• hydrophilic organic molecules
• general formula
– (CH2O)n n = number of carbon atoms
– for glucose, n = 6, so formula is C6H12O6

• names of carbohydrates often built from:

– word root ‘sacchar-’
– the suffix ’-ose’
– both mean ‘sugar’ or ‘sweet’
• monosaccharide or glucose
2-45
 Monosaccharides
• Simplest carbohydrates Glucose CH2OH
O
H H
– simple sugars H

HO OH H OH

H OH
• 3 important monosaccharides Galactose CH2OH

– glucose, galactose and fructose HO

O
H
H

– same molecular formula - C6H12O6 H

OH H
OH

• isomers H OH

– produced by digestion of complex Fructose

O
carbohydrates HOCH2 OH

• glucose is blood sugar H

H HO
CH2OH

OH H

2-46
Figure 2.16
 Disaccharides
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

• Sugar molecule Sucrose

CH2OH
O CH2OH O
composed of 2 H
H
OH H
H

H HO
H

monosaccharides
O
HO CH2OH

H OH OH H

• 3 important Lactose
CH2OH H OH

disaccharides HO
H
O
O
OH H
OH

OH H H
– sucrose - table sugar H H H
O
H

• glucose + fructose H OH CH2OH

– lactose - sugar in milk Maltose

CH2OH CH2OH
• glucose + galactose H O H H
O OH

– maltose - grain products H

OH H
O
H
OH H
HO H
• glucose + glucose
H OH H OH

2-47
Figure 2.17
 Polysaccharides
• long chains of glucose
• 3 polysaccharides of interest in humans
– Glycogen: energy storage polysaccharide in
animals
• made by cells of liver, muscles, brain, uterus, and vagina
• liver makes glycogen after a meal when glucose level is high,
then breaks it down later to maintain blood glucose levels

– Starch: energy storage polysaccharide in plants

• only significant digestible polysaccharide in the human diet

– Cellulose: structural molecule of plant cell walls

• fiber in our diet
2-48
 Glycogen
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

O O
O

CH2OH CH2OH
O

O O
O

O O
O
O
O

O
O
O O O
O

O O
O O
O

O O

O
O

CH2OH CH2OH CH2 CH2OH

O

O O
O

O
O

O O O O
O
O

O
O

O O O O O
O

(a) (b)

Figure 2.18
2-49
2-50
 Organic Molecules: Lipids
• hydrophobic organic molecule
– composed of carbon, hydrogen and oxygen
– with high ratio of hydrogen to oxygen

• Less oxidized than carbohydrates, and thus has

more calories/gram
• Five primary types in humans
– fatty acids
– triglycerides
– phospholipids
– eicosanoids
– steroids 2-51
 Fatty Acids
• Chain of 4 to 24 carbon atoms
– carboxyl (acid) group on one end, methyl group on the other and
hydrogen bonded along the sides

• Types
– saturated - carbon atoms saturated with hydrogen
– unsaturated - contains C=C bonds without hydrogen
– polyunsaturated – contains many C=C bonds
– essential fatty acids – obtained from diet, body can not synthesize
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

H H H H H H H H H H H H H H H
O
C C C C C C C C C C C C C C C C H
HO
H H H H H H H H H H H H H H H
Palmitic acid (saturated)
CH3(CH2)14COOH Figure 2.19 2-52
 Triglycerides (Neutral Fats)
• 3 fatty acids covalently bonded to glycerol molecule

• triglycerides at room temperature

– when liquid called oils
• often polyunsaturated fats from plants
– when solid called fat
• saturated fats from animals

• Primary Function - energy storage, insulation and shock

absorption (adipose tissue)

2-53
 Phospholipids
• similar to neutral fat CH3

except that one fatty CH3 N+ CH3

Nitrogen-
containing
acid replaced by a CH2
group
CH2
(choline)
phosphate group O

–
O P O
Phosphate Hydrophilic
group region (head)
• structural foundation O

CH2 CH CH2 Glycerol

of cell membrane O O

O C C O

• Amphiphilic (CH2)5 (CH2)12 Fatty acid

CH CH3
tails
– fatty acid “tails” are CH Hydrophobic
hydrophobic (CH2)5 region (tails)
– phosphate “head” is CH3

hydrophilic
(a)

(b)

Figure 2.20a,b 2-54

 Eicosanoids
• 20 carbon compounds derived from a fatty acid
called arachidonic acid
• hormone-like chemical signals between cells
• includes prostaglandins – produced in all
tissues
– role in inflammation, blood clotting, hormone action,
labor contractions, blood vessel diameter
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

COOH
Figure 2.21

2-55
OH OH
 Steroids and Cholesterol
• Steroid – a lipid with 17 of its carbon atoms in four
rings
• Cholesterol - the ‘parent’ steroid from which the
other steroids are synthesized
– cortisol, progesterone, estrogens, testosterone and bile
acids
– synthesized only by animals
• 15% from diet, 85% internally synthesized
– important component of cell membranes
– required for proper nervous system function

2-56
 Cholesterol
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

H 3C

CH3
CH3

CH3
CH3

HO

Figure 2.22 2-57

2-58
 Organic Molecules: Proteins
• Greek word meaning “of first importance”

– most versatile molecules in the body

• protein - a polymer of amino acids
• amino acid – central carbon with 3 attachments
– amino group (NH2), carboxyl group (COOH) and radical
group (R group)
– properties of amino acid determined by -R group

2-59
 Representative Amino Acids
Some nonpolar aa’s Some polar aa’s
Methionine Cysteine
H H H H

N N

H C CH2 CH2 S CH3 H C CH2 SH

C C
O OH O OH

Tyrosine Arginine
H H H H
N N
NH2+
H C CH2 OH H C (CH2)3 NH C

C C
NH2 Figure 2.23a
O OH O OH

(a)

• Note: they differ only in the R group

2-60
 Naming of Peptides
• peptide – any molecule composed of two or more
amino acids joined by peptide bonds
• peptide bond – joins the amino group of one amino
acid to the carboxyl group of the next
– formed by dehydration synthesis

• Peptides named for the number of amino acids

– dipeptides have 2
– tripeptides have 3
– oligopeptides have fewer than 10 to 15
– polypeptides have more than 15
– proteins have more than 50
2-61
 Protein Structure and Shape
• Primary structure
– sequence of amino acids (encoded in the genes)
• Secondary structure
– coiled or folded shape held together by hydrogen
bonds
– hydrogen bonds between slightly negative C=O
and slightly positive N-H groups
– most common secondary structures are:
• alpha helix – springlike shape
• beta sheet – pleated, ribbonlike shape

2-62
 Protein Structure and Shape
• Tertiary structure
– further bending and folding of proteins into globular and
fibrous shapes
• globular proteins –compact structure good for proteins
embedded in cell membrane or that move about in fluid
• fibrous proteins – slender filaments better suited for
roles as in muscle contraction and strengthening skin
• Quaternary structure
– associations of two or more separate polypeptide chains

2-63
 Structure of Proteins
example: hemoglobin

Amino acids

Primary structure Tertiary structure

Sequence of amino Folding and coiling

acids joined by due to interactions
peptide bonds among R groups and
C between R groups
and surrounding water
C
N
H
C

Secondary structure Beta

C
Quaternary structure
C C chain
Alpha helix or beta
sheet formed by Association of two
C
C hydrogen bonding Heme or more polypeptide
chains with each
N

groups
other
Alpha
chain
Alpha Beta
helix sheet Figure 2.24
2-64
 Protein Conformation and
Denaturation
• Conformation – unique three dimensional shape of
protein crucial to function
– some proteins can reversibly change their conformation
• enzyme function
• muscle contraction
• opening and closing of cell membrane pores

• Denaturation
– extreme conformational change that destroys function
• extreme heat or pH

2-65
 Protein Functions
• Structure
– keratin – tough structural protein
• gives strength to hair, nails, and skin surface
– collagen – durable protein contained in deeper layers of skin, bones,
cartilage, and teeth

• Communication
– some hormones and other cell-to-cell signals
– receptors to which signal molecules bind

• Membrane Transport
– channels in cell membranes that govern what passes through
– carrier proteins – transport solute particles to other side of membrane
– turn nerve and muscle activity on and off
2-66
 Protein Functions
• Catalysis
– enzymes

• Recognition and Protection

– immune recognition
– antibodies
– clotting proteins

• Movement
– motor proteins - molecules with the ability to change shape
repeatedly (like in muscles)

• Cell adhesion
– proteins bind cells together
– immune cells bind to cancer cells 2-67
– keeps tissues from falling apart
 Enzymes
• Enzymes - proteins that function as biological
catalysts
– permit reactions to occur rapidly at normal body
temperature

• Substrate - substance an enzyme acts upon

• Naming Convention
– named for substrate with -ase as the suffix
• amylase enzyme digests starch (amylose)

• Lowers activation energy - energy needed to get

reaction started
– enzymes facilitate molecular interaction 2-68
 Enzyme Structure and Action
1. Substrate approaches active site on enzyme molecule
2. Substrate binds to active site forming enzyme-substrate
complex
- highly specific fit –’lock and key’

3. Enzyme breaks covalent bonds between monomers in

substrate
- adding H+ and OH- from water – Hydrolysis

4. Reaction products released

5. Enzyme remains unchanged and is ready to repeat the
process
2-69
Enzymatic Reaction Steps
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Sucrose (substrate)
Enzyme and
O
substrate

Active site

Sucrase (enzyme)

2 Enzyme–substrate
complex

Glucose Fructose
3 Enzyme
and reaction
products
Figure 2.27

2-70
 Enzymatic Action
• Re-usability of enzymes
– enzymes are not consumed by the reactions

• Astonishing speed
– one enzyme molecule can consume millions of substrate
molecules per minute

• Factors that change enzyme shape

– pH and temperature
– alters or destroys the ability of the enzyme to bind to
substrate
– enzymes vary in optimum pH
• salivary amylase works best at pH 7.0
• pepsin works best at pH 2.0
– temperature optimum for human enzymes – body
2-71
temperature (37 degrees C)
 Organic Molecules:
Nucleotides

• ATP – best known nucleotide

– adenine (nitrogenous base)
– ribose (sugar)
– phosphate groups (3)

2-72
 ATP (Adenosine Triphosphate)
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

Adenine Adenine
NH2 NH2

C C
N N
N C N C
CH CH
HC C HC C
N N
N N
Adenosine
Ribose Ribose
Triphosphate

O O O Monophosphate

–O P O P O P O CH2 O O CH2 O

–O –O –O HO P O
H H H H H H H H

OH OH O OH

(a) Adenosine triphosphate (ATP) (b) Cyclic adenosine monophosphate (cAMP)

Figure 2.29a, b
ATP contains adenine, ribose and 3 phosphate groups 2-73
 Adenosine Triphosphate (ATP)
• body’s most important energy-transfer molecule

• briefly stores energy gained from exergonic reactions

– releases it within seconds for physiological work

• holds energy in covalent bonds

– 2nd and 3rd phosphate groups have high energy
bonds
– most energy transfers to and from ATP involve
adding or removing the 3rd phosphate

2-74
Sources and Uses of ATP
are converted to
Glucose + 6 O2 6 CO2 + 6 H2O

which releases
energy

which is used for

ADP + Pi ATP

which is then available for

Muscle contraction
Ciliary beating
Active transport
Synthesis reactions
etc.
Figure 2.30 2-75