LECTURE PRESENTATIONS

For BIOLOGY, TWELFTH EDITION

Sylvia S. Mader, Michael Windelspecht
Michael Windelspecht

Chapter 6

Metabolism: Energy
and Enzymes

Lectures by Dr. Sabika Allehdan, PhD

Erin Barley
 Outline
6.1 Cells and the Flow of Energy
6.2 Metabolic Reactions and Energy Transformations
6.3 Metabolic Pathways and Enzymes
6.4 Oxidation-Reduction Reactions and Metabolism

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 6.1 Cells and the Flow of Energy
• Energy is the ability to do work or bring about a change.
– Kinetic energy
• Energy of motion as when water going over a waterfall, a ball
rolls down a hill.
• Mechanical energy of motion
– Potential energy
• Stored energy whose capacity to accomplish work is not being
used at the moment.
• Chemical energy

– The food we eat has potential energy (energy stored in chemical

bonds can be converted into various types of kinetic energy.
Chemical energy associated with the interaction of atoms in a
molecule (i.e., carbohydrates, proteins, and fat).
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 Flow of Energy

A plant converts solar energy to the stored chemical energy of nutrient molecules. The moose
converts a portion of this chemical energy to the mechanical energy of motion. Eventually, all
solar energy absorbed by the plant dissipates as heat.

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 Two Laws of Thermodynamics
• In nature, energy flows in biological systems and
through cells
• First law
• Law of conservation of energy
• Energy cannot be created or destroyed, but can be changed
from one form to another
• Example – Photosynthesizing leaves capture solar energy
• Some energy is used to form carbohydrates from CO2 and
H2O
• Much of the energy dissipates as heat

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 Two Laws of Thermodynamics
• Second law (applies to living systems)
• When energy is changed from one form to another, there is
a loss of energy that is available to do work
• No process requiring a conversion of energy is ever 100%
efficient
• Most of the energy is lost as dissipated heat, thus it is not
available to do work
• Example – cells are capable of about 40% efficiency; the
remaining energy is given off as heat to surrounding
environment
• Heat can never be converted back to another form of
energy
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 Two Laws of Thermodynamics

6 CO2 + 6 H2O + solar Energy C6H12O6 + 6O2

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 Cells and Entropy
• Entropy: Measure of disorder or randomness in a
system, it is used to indicate the relative amounts of
disorganization
• Every process in cells increases the total entropy in the
universe
• Therefore, less energy is available to do useful work
• Organized, usable energy has a low entropy
• Disorganized energy, such as heat, has a high entropy

• No energy conversion is ever 100% efficient, because

much energy is dispersed as heat, increasing entropy
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 Cells and Entropy
• Example – glucose tends to break apart into carbon
dioxide and water over time:
• Glucose is more organized and less stable than its
breakdown products
• Compare this to a neat room, which is more organized but
less stable than a messy room
• Energy is required to make a messy room more neat
• Similarly, the input of energy from photosynthesis (the
sun) makes glucose from carbon dioxide and water
• Living organisms depend on a constant supply of solar
energy
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 Cells and Entropy

The second law of thermodynamics tells us that a. glucose, which is more organized, tends
to break down to carbon dioxide and water, which are less organized. b. similarly, hydrogen
ions (H+) on one side of a membrane tend to move to the other side, so that the ions are
randomly distributed. Both processes result in an increase in entropy.

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 6.2 Metabolic Reactions and Energy
Transformations
• Metabolism-sum of cellular chemical reactions in cell
• Reactants are substances that participate in a reaction
• Products are substances that form as result of a reaction
• A reaction occurs spontaneously (no energy input) if it increases the
entropy of the universe
• Two main types of metabolism:

• Anabolism – complex molecules are synthesized from

simpler substances (requires energy)
• Catabolism – larger molecules are broken down into smaller
ones (releases energy)

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 Exergonic Reactions
• Free energy (∆G) is the amount of energy that is
free to do work after a chemical reaction has
occurred
• Change in free energy is determined by subtracting the
free energy content of the reactants from that of the
products
• Exergonic reactions
• Products have less free energy than reactants (i.e., release
energy)
• They occur spontaneously
• ΔG has a negative value
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 Endergonic Reactions
• Endergonic reactions
• Products have more free energy than reactants (i.e., require
energy)
• These are nonspontaneous
• Example- protein and carbohydrate synthesis in the body;
must be coupled with exergonic reactions
• ΔG has a positive value
• Many biological processes use ATP as an energy carrier
between exergonic and endergonic reactions

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Copyright © McGraw-Hill Education
 ATP: Energy for Cells
• Adenosine triphosphate (ATP)
• High energy compound used to drive metabolic reactions
• ATP not stored by cells
• Constantly being generated from ADP + inorganic P + energy → ATP

• Composed of adenine, ribose and 3 phosphate groups

• Coupled reactions
• Energy released by an exergonic reaction (or reactions) is
captured in ATP
• ATP is then used to drive an endergonic reaction

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 The ATP Cycle

In cells, ATP carries energy between exergonic reactions and endergonic reactions. When a
phosphate group is removed by hydrolysis, ATP releases the appropriate amount of energy
for most metabolic reactions.

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 The ATP Cycle
• The ATP cycle is powered by the breakdown of glucose
and other biomolecules during cellular respiration
• According second law of thermodynamics, this process
is not very efficient
• Only 39% of the free energy stored in the chemical
bonds of a glucose molecule is transformed to ATP
• The rest is lost as heat

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 ATP
• Biological advantages to the use of ATP
• It provides a common and universal energy currency
used in many types of reactions
• When ATP becomes ADP + the amount of energy
released is sufficient for biological function with
little waste of energy (~ 7.3 kcal per mole)
• ATP breakdown can be coupled to endergonic
reactions that prevents energy waste

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 Coupled Reactions
• How ATP acts as carrier of chemical energy?
• ATP breakdown is coupled to the energy-requiring reaction such
that both the energetically favorable and unfavorable reactions
occur in the same place, at the same time
• Two main ways of couple ATP hydrolysis to an energy-
requiring reaction:
• ATP is used to energize a reactant
• Or ATP is used to change the shape of a reactant
• Both can be achieved by phosphorylation
• Examples:
• Movement of polar ion across the non-polar membrane through carrier
protein. Change of shape of carrier protein by negatively charged phosphate
• Attachment of amino acids to a growing polypeptide chain

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 Functions of ATP in Cells
• In living systems, ATP can be used for
• Chemical work
• ATP supplies the energy needed to synthesize
macromolecules (anabolism) that make up the cell, and
therefore the organism
• Transport work
• ATP supplies the energy needed to pump substances across
the plasma membrane
• Mechanical work
• ATP supplies the energy needed to permit muscles to
contract, cilia and flagella to beat, chromosomes to move, etc
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 Use of ATP during Muscle Contraction

Muscle contraction occurs only when it is coupled to ATP breakdown

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 Use of ATP during Muscle Contraction

Muscle contraction occurs only when it is coupled to ATP breakdown

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 6.3 Metabolic Pathways and Enzymes
• Enzymes is protein catalysts that speed chemical reactions
without the enzyme being affected by the reaction.
• Ribozymes are RNA molecules that function as biological
catalysts; involved in RNA and protein synthesis
• The reactants of an enzymatically accelerated reaction are called
substrates
• Each enzyme accelerates a specific reaction
• Each reaction requires a unique and specific enzyme
• End product will not appear unless ALL enzymes are present
and functional

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 Metabolic Pathways
• Reactions normally occur in a sequence
• Products of an earlier reaction become reactants of a later
reaction
• Such linked reactions form a metabolic pathway
• It begins with a particular reactant, proceeds through several
intermediates, and terminates with a particular end product
• In other words, the product of the first reaction is the substrate
of the second and so on, except in the case of G

A→B → C → D → E → F → G
“A” is Initial B, C, D, E, and F “G” is End
Reactant are Intermediates Product
or Substrate
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 Enzyme-Substrate Complex
• The active site of an enzyme complexes with the
substrates
• It causes the active site to change shape
• The shape change forces substrates together, initiating
bond formation
• Active site returns to its original state after the
product(s) is released
• Induced fit model
• Enzyme is induced to undergo a slight alteration to
achieve optimum fit for the substrates
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 Enzyme-Substrate Complex
• Synthesis (Anabolism):
• Enzyme complexes with two substrate molecules
• Substrates are joined together and released as single
product molecule
• Degradation (Catabolism):
• Enzyme complexes with a single substrate molecule
• Substrate is broken apart into two product molecules
• Only a small amount of enzyme is needed in a cell
because enzymes are not consumed during catalysis
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 Enzymatic Actions

Enzymes have an active site where the substrate (s) specifically fit together, so that the
reaction will occur. Following the reaction, the product or products are released, and the
enzyme is free to act again. Certain enzymes carry out degradation, and others carry out
synthesis.

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 Energy of Activation
• Molecules frequently do not react with one another unless they
are activated in some way
• Energy must be added to at least one reactant to initiate the
reaction
• Energy of activation (Ea) is energy that must be added to cause
molecules to react with one another
• Enzyme Operation:
• Enzymes operate by lowering the energy of activation
• Brings the substrates into contact with one another and even participates in
the reaction
• This influences the rate of reaction and is why enzymes are catalysts of
chemical reactions

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 Energy of Activation

Enzymes speed the rate of the reactions, because they lower the amount of energy required
for the reactants to activate. Even spontaneous reactions like this one, in which the energy
of the product is less than the energy of the reactant, speed up when an enzyme is present.

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 Factors Affecting Enzymatic Speed
• Rate of reaction: amount of product produced per unit
time
• Depends on how much substrate is available for active
site of enzyme
• It can be increased by increasing amount of substrate
and enzyme
• Any factor affecting shape of active site like temp and
pH can cause denaturation
• Cofactors are additional molecules which help by
binding substrate to active site

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 Factors Affecting Enzymatic Speed
• Substrate concentration
• Enzyme activity increases with substrate concentration
due to more collisions between substrate molecules and
the enzyme
• When the active sites of the enzyme are filled, with
increasing substrate, the enzyme’ s rate of activity
cannot increase any more
• Amount of active enzyme can also increase or limit the
rate of an enzymatic reaction

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 Factors Affecting Enzymatic Speed
• Temperature
• Enzyme activity increases with temperature
• Warmer temperatures cause more effective collisions
between enzyme and substrate
• Hot temperatures destroy enzymes, how?
• Denaturation – enzyme ’s shape changes and it can
no longer bind to its substrate efficiently
• Siamese cats have a mutation that causes enzymes to
be active at cooler temperatures that affects coloration

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 The effect of temperature on rate of
reaction

a. Usually, the rate of an enzymatic reaction doubles with every 10 oC rise in temperature.
This enzymatic reaction is maximum at about 40 oC; then it decreases until the reaction
stops altogether, because the enzyme has become denture.

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 Factors Affecting Enzymatic Speed
• Optimal pH
• Most enzymes are optimized for a particular pH
• Changes in pH can make and break intra- and
intermolecular bonds, and/or hydrogen bonds, which
alters the globular shape of the enzyme
• pH change can alter the ionization of R side chains
• Under extreme conditions of pH, the enzyme
becomes inactive (due to altered shape)

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 The Effect of pH on Rate of Reaction

The effect of pH on rate of reaction. The optimal pH for pepsin, an enzyme

that acts in the stomach, is about 2 , while the optimal pH for trypsin, an
enzyme that acts in the small intestinal, is about 8. Enzyme shape is best
maintained at the optimal pH, which allows it to function best and bind with
its substrate.
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 Factors Affecting Enzymatic Speed
• Cells can regulate the presence/absence of an enzyme
and the concentration of an enzyme
• Cells can activate or deactivate some enzymes
• Many enzymes require the presence of an inorganic or
non-protein organic molecules at the active site in
order to work properly; these necessary molecules are
called cofactors
• The inorganic ions include metals such as copper,
zinc, or iron
• The nonprotein organic molecules are called
coenzymes

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 Factors Affecting Enzymatic Speed
• FAD and and are cofactors, the first two in cellular
respiration, the third in photosynthesis.
• Vitamins are small organic compounds required in the
diet for the synthesis of coenzymes.
• Vitamin Niacin is part of NAD+ and riboflavin (B2)
is part of FAD
• Niacin deficiency will result in skin disease Pellagra
• Riboflavin (B2) deficiency will result in cracks at the
corner of mouth

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 Cofactors at Active Site

a. Cofactors, including inorganic ions and organic coenzymes, may

participate in the reaction at b the active site.

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 Enzyme Inhibition
• Reversible enzyme inhibition
– A substance known as an inhibitor binds to an enzyme and decreases its
activity.
• Competitive inhibition – The substrate and the inhibitor are both
able to bind to active site and they compete with one another. The
product forms only when the substrate binds to the active site.
• Noncompetitive inhibition – The inhibitor does not bind at the
active site, but at an allosteric (allo means other) site.
– A change in shape initiated by inhibitor binding to the
allosteric site changes the shape of the active site, making it
unable to bind substrate.
• Feedback inhibition – The end product of a pathway inhibits
the pathway’s first enzyme

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 Noncompetitive Inhibition of an Enzyme

In the pathway, A-E are substrates , E1-E5 are enzymes , and F is the end product of the pathway
that inhibits enzyme E1. this negative feedback is useful, because it prevents wasteful production
of product F when it is not needed.
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 Irreversible Enzyme Inhibition
• Materials that irreversibly inhibit an enzyme are
known as poisons
• Cyanides inhibit enzymes resulting in all ATP
production
• Penicillin inhibits an enzyme unique to certain
bacteria
• Heavy metals irreversibly bind with many enzymes
• Nerve gas (Sarin) irreversibly inhibits enzymes
required by nervous system

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 6.4 Electron Transfer in Redox Reactions
• Oxidation-reduction (redox) reactions

• Electrons pass from one molecule to another.

• The reaction that involve the gain and loss of electrons are
called oxidation-reduction reactions

• The molecule that loses an electron is oxidized

• The molecule that gains an electron is reduced

• Oxidation – loss of an electron

• Reduction – gain of an electron

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 6.4 Electron Transfer in Redox Reactions
• Oxidation-reduction (redox) reactions

• Both take place at same time, therefore called Redox

reaction

• One molecule (or atom) accepts the electron given up by the

other.

• Example: In the production of NaCl, sodium is oxidized

and chlorine is reduced;

• OIL (oxidation is loss)

• RIG (reduction is gain)

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 6.4 Electron Transfer in Redox Reactions
• Oxidation-reduction (redox) reactions

• The term is also applied to covalent reactions in cell

• In this case, oxidation is loss of Hydrogen atoms and

reduction is gain of hydrogen atoms

• When a molecules loses a hydrogen atom , it has lost

an electron and gain of hydrogen atom is gain of
electron

• Photosynthesis and cellular respiration

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 6.4 Electron Transfer in Redox Reactions

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