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Energy and Living Things

• Living systems appear to contradict the Second
Law of Thermodynamics:
– Energy in the universe has direction and that
it has been, and always will be, degraded to
heat. This increase in disorder, or
randomness, in any closed system is termed
entropy.
• Living systems decrease their entropy by
increasing the molecular orderliness of their
structure.
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 Chapter 4

White-tailed deer (Odocoileus virginianus) foraging

on fallen apples.
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Cellular Metabolism
• All cells must obtain energy, as well to:
– Synthesize internal structures
– Control activity
– Guard their boundaries
• Cellular metabolism is the chemical processes that
occur within living cells to accomplish these tasks.
– Concept of energy fundamental to all life
processes
– Energy cannot be seen
• Can be identified only by how it affects matter
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 Energy Transfer

Figure 4.1 Solar energy sustains virtually all life on

the Earth. With each energy transfer, about 90% of
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the energy is lost as heat.
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Energy and the Laws of Thermodynamics

• Energy exists in either of two states.
– Kinetic energy
• Energy of motion
– Potential energy
• Stored energy
• Energy that is not doing work but has the
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 First Law of Thermodynamics
• First Law of Thermodynamics
– Energy cannot be created or destroyed.
– Energy can change from one form to
another.
– Total amount of energy remains the same.

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Second Law of Thermodynamics

• Second Law of Thermodynamics
– Concerned with the transformation of
energy.
– A closed system moves toward increasing
disorder (entropy) as energy is dissipated
from the system.
– Living systems are open systems.
• Maintain organization and increase it
during development and growth.
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 Free Energy
• Free energy is the energy in a system available
to do work.
– In molecules, it is the energy present in
chemical bonds minus the energy that
cannot be used.

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Exergonic Reactions
• Exergonic reactions
– Release free energy.
– Majority of reactions in cells are of this type.
– Occur spontaneously and proceed “downhill.”

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 Endergonic Reactions
• Endergonic reactions
– Reactions requiring the addition of free energy.
– Must be “pushed uphill.”
– ATP is the molecule used by organisms to power
endergonic reactions.

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The Role of Enzymes

• Activation energy
– Energy that must be supplied to stress and
break chemical bonds for reactions to occur.
– Enzymes
• Catalyze (speed up) chemical reactions.
• Not altered or destroyed in the reactions.
• Affect only the reaction rate.
• Do not alter the free energy change of a
reaction.
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 Activation Energy

Figure 4.3 Energy changes during enzyme catalysis of a

substrate. The overall reaction proceeds with a net release of
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The Nature of Enzymes

• Enzymes are complex molecules that vary in size.
– Many are pure proteins.
– Some enzymes require small nonprotein groups,
cofactors, to perform enzymatic function.
• Ex: Metallic ions
– If the cofactor is organic, it is called a coenzyme.
• Contain groups derived from vitamins that must
be supplied by diet
• Vitamin component cannot be synthesized in
animals
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– RNA is now known to possess enzymatic activity.
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 Action of Enzymes
• An enzyme functions by associating in a highly
specific way with its substrate.
– Reactants in enzymatic reactions called
substrates
– Active site: Region of an enzyme to which
the substrate binds
• Located in cleft or pocket
• Has flexible surface that enfolds and
conforms to the substrate
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Enzyme–Substrate Complex
• Binding of enzyme to substrate forms an
enzyme–substrate complex (ES complex).
– Substrate is secured by covalent bonds to
active site.
– ES complex is not strong and will quickly
dissociate.
– Enzyme provides unique chemical
environment that stresses chemical bonds in
substrate.
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 Enzyme Function

Figure 4.4 How an enzyme works. (A)The ribbon model. (B) The space-filling model
shows the enzyme lysozyme bearing a pocket with the active site. (C) The enzyme–
substrate complex (ES complex).

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Specificity of Enzymes
• The specificity of enzymes is a distinctive attribute.
– Enzymes catalyze only one reaction.
– No side reactions or byproducts result.
– Some variation in the degree of specificity exist.
• Examples:
–Succinic dehydrogenase only catalyzes the
oxidation of succinic acid.
–Proteases act on almost any protein.
»Each protease has its particular point of
attack (like pepsin and trypsin).
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 Specificity of Trypsin

Figure 4.5 Substrate specificity of trypsin. It splits only peptide bonds

adjacent to lysine or arginine, but does the same in many different proteins.

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Lifespan of an Enzyme
– Enzymes may catalyze billions of reactions
until worn out and degraded by scavenger
enzymes in cell.
– Some enzymes undergo successive catalytic
cycles at speeds of up to a million cycles per
minute, but most operate at slower rates.
– Many enzymes are repeatedly activated and
inactivated.

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 Enzyme-Catalyzed Reactions
• Enzyme-catalyzed reactions are reversible
reactions.
– Most reactions tend to go predominantly in
one direction.
– Net direction of a reaction depends on
relative energy contents of the substances
involved.
• If there is little change in chemical bond
energy of substrate and products, then
the reaction is more easily reversible.
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Reversing a Reaction
• If large quantities of energy are released as the
reaction proceeds, more energy must be
provided to drive the reaction in the reverse
direction.
• Many enzyme-catalyzed reactions are in
practice irreversible unless coupled to another
that makes enough energy available to reverse
the reaction coupled to it.
– Examples of this are the synthesis and
degradation of ATP in cells.
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 Enzyme Regulation
• The function of many enzymes is tightly controlled.
– Quantity of enzymes regulated by molecules that
switch on or off enzyme synthesis
– Activity of enzymes controlled by presence or
absence of metabolites that cause conformational
changes in enzymes
• Activating or inhibiting the enzyme
• Feedback inhibition occurs when the end
product of a metabolic pathway inhibits the first
enzyme in the pathway
– Activity of enzymes may be controlled by presence
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Enzyme Activation

Figure 4.6 Enzyme regulation. (A) The active site loosely fits its substrate in the
absence of an activator. (B) Presence of activator allows enzyme to bind the substrate
and becomes catalytically active.

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 Chemical Energy Transfer by ATP
• Endergonic reactions are coupled with
exergonic reactions by the energy-rich
molecule ATP.
• ATP (adenosine triphosphate)
– Drives energetically unfavorable reactions
– Formed primarily in mitochondria
– Most free energy in ATP resides in two
phosphoanhydride (high-energy) bonds
between the three phosphate groups
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ATP Structure

Figure 4.7 (A) Structure of ATP. (B) ATP formation from ADP and AMP.
Figure 4.8 Space-filling model of ATP.

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 ATP Drives Reactions
• Coupled reaction
– System involving two reactions linked by an
energy shuttle (ATP)
• High-energy bonds of ATP are rather unstable,
weak bonds—easily broken!
• Energy of ATP is readily released when ATP is
hydrolyzed in cellular reactions
– ATP + H2O → ADP + Pi

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Energy-Coupling Agent
• ATP is an energy-coupling agent not a fuel;
therefore, it is not stored in the body!
• ATP is formed as needed and consumed
immediately.
– Metabolism is mostly self-regulating.
– ATP (adenosine triphosphate) changes to
ADP (adenosine diphosphate) then to AMP
(adenosine monophosphate), which gets
recharged to become ATP again.
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 Coupled Reaction

Figure 4.9 A coupled reaction. The endergonic conversion of

substrate A to product A will not occur spontaneously but requires
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an input of energy.

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Electron Transport & Chemical Bond Energy

• Cells meet chemical energy requirements from
oxidation–reduction reactions.
– Transfer of electrons occurs from an electron
donor (reducing agent) to electron acceptor
(oxidizing agent).
– As fuel molecules are broken down,
hydrogen atoms (electrons and protons) are
passed from electron donors to electron
acceptors with a release of energy.
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 Accepting Electrons
• When electrons are accepted by an oxidizing agent:
– Energy is released as electrons move to a more stable position.
• ATP can be produced when electrons flow through a series of
carrier molecules
– Energy is gradually released.
– Ultimately, electrons are transferred to the final electron acceptor.
– The nature of the final acceptor is key in determining the overall
efficiency of cellular metabolism.

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Oxidation–Reduction Reaction

Figure 4.10 A redox pair. The molecule at left is oxidized by the loss of an
electron. The molecule at right is reduced by gaining an electron.

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 Aerobic vs. Anaerobic Metabolism
• Heterotrophs divided into groups based on the efficiency of energy
production during cellular respiration.
– Aerobes: Use molecular oxygen as the final electron acceptor.
• Almost 20 times more energy is released compared to
anaerobes
• Advantage is the need for smaller quantity of food to
maintain given rate of metabolism
– Anaerobes: Use other molecules (e.g., pyruvic acid) as final
electron acceptor.
• Play important roles in specialized habitats
• Occurs when oxygen is absent or present in low quantities
• Energy yield is much lower than aerobic respiration
• Final electron acceptor still contains most of the energy
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stored
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Cellular Respiration
• Overview of Respiration
– Cellular respiration is aerobic metabolism.
• Oxidation of fuel molecules (removal of
electrons) to produce energy with
molecular oxygen acting as the final
electron acceptor.
• Hans Krebs, the British biochemist,
described three stages of cellular
respiration.
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