1) The document discusses key concepts about metabolism from chapters 5.1-5.4 of a biology textbook, including how enzymes work to catalyze reactions and the roles of ATP, activation energy, and temperature and pH in metabolism.
2) It explains how alcohol is broken down by the liver enzyme alcohol dehydrogenase and how energy flows through biological systems in one direction according to the laws of thermodynamics.
3) The summary highlights that ATP couples exergonic and endergonic reactions to do cellular work and that enzymes lower activation energies to speed up metabolic reactions.
Beyond Boundaries: Leveraging No-Code Solutions for Industry Innovation
Metabolism and Energy Flow
1. Albia Dugger • Miami Dade College
Cecie Starr
Christine Evers
Lisa Starr
www.cengage.com/biology/starr
Chapter 5
Ground Rules of Metabolism
(Sections 5.1 - 5.4)
2. 5.1 A Toast to
Alcohol Dehydrogenase
• Metabolic processes build and break down organic molecules
such as ethanol and other toxins
• Alcohol breakdown directly damages liver cells, and interferes
with normal processes of metabolism
• Currently the most serious drug problem on college
campuses is binge drinking
3. Alcohol Metabolism
• The enzyme
alcohol
dehydrogenase
helps the liver
break down toxic
alcohols (ethanol)
4. 5.2 Energy and the World of Life
• There are many forms of energy:
• Kinetic energy, potential energy
• Light, heat, electricity, motion
• Energy cannot be created or destroyed (first law of
thermodynamics)
• Energy can be converted from one form to another and thus
transferred between objects or systems
5. Energy Disperses
• Energy tends to disperse spontaneously (second law of
thermodynamics)
• A bit disperses at each energy transfer, usually as heat
• Entropy is a measure of how dispersed the energy of a
system has become
6. Key Terms
• energy
• The capacity to do work
• kinetic energy
• The energy of motion
• entropy
• Measure of how much the energy of a system is dispersed
7. Key Terms
• first law of thermodynamics
• Energy cannot be created or destroyed
• second law of thermodynamics
• Energy tends to disperse spontaneously
9. Entropy
• Entropy tends to
increase, but the total
amount of energy in any
system always stays the
same
10. Fig. 5.3, p. 76
Entropy
Time
heat
energy
Stepped Art
Entropy
11. Work
• Work occurs as a result of an energy transfer
• A plant converts light energy to chemical energy in
photosynthesis
• Most other cellular work occurs by transfer of chemical energy
from one molecule to another (such as transferring chemical
energy from ATP to other molecules)
12. Energy’s One-Way Flow
• Living things maintain their organization only as long as they
harvest energy from someplace else
• Energy flows in one direction through the biosphere, starting
mainly from the sun, then into and out of ecosystems
• Producers and then consumers use energy to assemble,
rearrange, and break down organic molecules that cycle
among organisms throughout ecosystems
13. Energy Conversion
• It takes 10,000 pounds
of feed to raise a 1,000-
pound steer
• About 15% of energy in
food builds body mass;
the rest is lost as heat
during energy
conversions
14. Energy Flow
• Energy flows from the
environment into living
organisms, and back to
the environment
• Materials cycle among
producers and
consumers
15. Fig. 5.5, p. 77
Consumers
animals, most fungi,
many protists, bacteria
nutrient cycling
Producers
plants and other
self-feeding organisms
sunlight
energy
Energy Flow
17. Potential Energy
• Energy’s spontaneous dispersal is resisted by chemical bonds
• Energy in chemical bonds is a type of potential energy,
because it can be stored
• potential energy
• Stored energy
18. Key Concepts
• Energy Flow
• Organisms maintain their organization only by continually
harvesting energy from their environment
• ATP couples reactions that release usable energy with
reactions that require it
20. 5.3 Energy in the Molecules of Life
• Every chemical bond holds energy – the amount of energy
depends on which elements are taking part in the bond
• Cells store and retrieve free energy by making and breaking
chemical bonds in metabolic reactions, in which reactants
are converted to products
21. Key Terms
• reaction
• Process of chemical change
• reactant
• Molecule that enters a reaction
• product
• A molecule that remains at the end of a reaction
22. Chemical Bookkeeping
• In equations that represent chemical reactions, reactants are
written to the left of an arrow that points to the products
• A number before a formula indicates the number of molecules
• The same number of atoms that enter a reaction remain at
the reaction’s end
26. Energy In, Energy Out
• In most reactions, free energy of reactants differs from free
energy of products
• Reactions in which reactants have less free energy than
products are endergonic – they will not proceed without a
net energy input
• Reactions in which reactants have greater free energy than
products are exergonic – they end with a net release of free
energy
27. Key Terms
• endergonic
• “Energy in”
• Reaction that converts molecules with lower energy to
molecules with higher energy
• Requires net input of free energy to proceed
• exergonic
• “Energy out”
• Reaction that converts molecules with higher energy to
molecules with lower energy
• Ends with a net release of free energy
29. Fig. 5.7, p. 78
Freeenergy
energy out
energy in
2H2O
O22H2
1
2
2H2O
Energy In, Energy Out
30. Why Earth Does Not Go Up in Flames
• Earth is rich in oxygen—and in potential exergonic reactions;
why doesn’t it burst into flames?
• Luckily, energy is required to break chemical bonds of
reactants, even in an exergonic reaction
• activation energy
• Minimum amount of energy required to start a reaction
• Keeps exergonic reactions from starting spontaneously
32. Fig. 5.8, p. 79
O2
Freeenergy
2H2
Activation energy
Products: 2H2ODifference between
free energy of
reactants and products
Reactants:
Activation Energy
34. ATP—The Cell’s Energy Currency
• ATP is the main currency in a cell’s energy economy
• ATP (Adenosine triphosphate)
• Nucleotide with three phosphate groups linked by high-
energy bonds
• An energy carrier that couples endergonic with exergonic
reactions in cells
36. Fig. 5.9a, p. 79
A Structure of ATP.
ribose
adenine
three phosphate
groups
ATP
37. Phosphorylation
• When a phosphate group is transferred from ATP to another
molecule, energy is transferred along with the phosphate
• Phosphate-group transfers (phosphorylations) to and from
ATP couple exergonic reactions with endergonic ones
• phosphorylation
• Addition of a phosphate group to a molecule
• Occurs by the transfer of a phosphate group from a donor
molecule such as ATP
39. Fig. 5.9b, p. 79
B After ATP loses one phosphate group, the nucleotide is
ADP (adenosine diphosphate); after losing two phosphate
groups, it is AMP (adenosine monophosphate)
ribose
adenine
AMP
ATPADP
ATP and ADP
40. ATP/ADP Cycle
• Cells constantly use up ATP to drive endergonic reactions, so
they constantly replenish it by the ATP/ADP cycle
• ATP/ADP cycle
• Process by which cells regenerate ATP
• ADP forms when ATP loses a phosphate group, then ATP
forms again as ADP gains a phosphate group
42. Fig. 5.9c, p. 79
energy out
ADP + phosphate
energy in
C ATP forms by endergonic reactions. ADP forms again
when ATP energy is transferred to another molecule
along with a phosphate group. Energy from such
transfers drives cellular work.
ATP/ADP Cycle
44. 5.4 How Enzymes Work
• Enzymes makes a reaction run much faster than it would on
its own, without being changed by the reaction
• catalysis
• The acceleration of a reaction rate by a molecule that is
unchanged by participating in the reaction
• Most enzymes are proteins, but some are RNAs
45. Substrates
• Each enzyme recognizes specific reactants, or substrates,
and alters them in a specific way
• substrate
• A molecule that is specifically acted upon by an enzyme
46. Active Sites
• Enzyme specificity occurs because an enzyme’s polypeptide
chains fold up into one or more active sites
• An active site is complementary in shape, size, polarity, and
charge to the enzyme’s substrate
• active site
• Pocket in an enzyme where substrates bind and a reaction
occurs
49. Fig. 5.10a, p. 80
active site
enzyme
A Like other enzymes,
hexokinase’s active sites bind
and alter specific substrates. A
model of the whole enzyme is
shown to the left.
An Active Site
51. Fig. 5.10b, p. 80
reactant(s)
B A close-up shows glucose
and phosphate meeting inside
the enzyme’s active site. The
microenvironment of the site
favors a reaction between the
two substrate molecules.
An Active Site
53. Fig. 5.10c, p. 80
product(s)
C Here, the glucose has
bonded with the phosphate.
The product of this reaction,
glucose-6-phosphate, is
shown leaving the active site.
An Active Site
54. Lowering Activation Energy
• Enzymes lower activation energy in four ways:
• Bringing substrates closer together
• Orienting substrates in positions that favor reaction
• Inducing the fit between a substrate and the enzyme’s
active site (induced-fit model)
• Shutting out water molecules
• induced-fit model
• Substrate binding to an active site improves the fit
between the two
56. Fig. 5.11, p. 80
Freeenergy
Reactants
Products
Transition state
Activation energy
with enzyme
Activation energy
without enzyme
Time
Lowering Activation Energy
58. Effects of Temperature, pH, and Salinity
• Each type of enzyme works best within a characteristic range
of temperature, pH, and salt concentration:
• Adding heat energy boosts free energy, increasing
reaction rate (within a given range)
• Most human enzymes have an optimal pH between 6 and
8 (e.g. pepsin functions only in stomach fluid, pH 2)
• Too much or too little salt disrupts hydrogen bonding that
holds an enzyme in its three-dimensional shape
60. Fig. 5.12, p. 81
Temperature
Enzymeactivity
temperature-
sensitive
tyrosinase
normal
tyrosinase
40°C (104°F)30°C (86°F)20°C (68°F)
Enzymes and Temperature
64. Help From Cofactors
• Most enzymes require cofactors, which are metal ions or
organic coenzymes in order to function
• cofactor
• A metal ion or a coenzyme that associates with an enzyme
and is necessary for its function
• coenzyme
• An organic molecule that is a cofactor
65. Coenzymes and Cofactors
• Coenzymes may be modified by taking part in a reaction
• Example: NAD+
becomes NADH by accepting electrons
and a hydrogen atom in a reaction
• Cofactors are metal ions
• Example: The iron atom at the center of each heme
• In the enzyme catalase, iron pulls on the substrate’s
electrons, which brings on the transition state
66. Antioxidants
• Cofactors in some antioxidants help them stop reactions
with oxygen that produce free radicals (harmful atoms or
molecules with unpaired electrons)
• Example: Catalase is an antioxidant
• antioxidant
• Substance that prevents molecules from reacting with
oxygen
67. Key Concepts
• How Enzymes Work
• Enzymes tremendously increase the rate of metabolic reactions
• Cofactors assist enzymes, and environmental factors such as
temperature, salt, and pH can influence enzyme function
Figure 5.1 Alcohol metabolism. Alcohol dehydrogenase helps the body break down toxic alcohols such as ethanol. This enzyme makes it possible for humans to drink beer, wine, and other alcoholic beverages
Figure 5.2 Demonstration of a familiar type of energy: motion, or kinetic energy.
Figure 5.3 Entropy. Entropy tends to increase, but the total amount of energy in any system always stays the same
Figure 5.3 Entropy. Entropy tends to increase, but the total amount of energy in any system always stays the same
Figure 5.4 It takes more than 10,000 pounds of soybeans and corn to raise a 1,000-pound steer. Where do the other 9,000 pounds go? About half of the steer’s food is indigestible. The animal’s body breaks down molecules in the remaining half to access energy stored in chemical bonds. Only about 15% of that energy goes toward building body mass. The rest is lost during energy conversions, as heat.
Figure 5.5 Energy flows from the environment into living organisms, and then back to the environment. The flow drives a cycling of materials among producers and consumers.
Figure 5.6 Chemical bookkeeping. In equations that represent chemical reactions, reactants are written to the left of an arrow that points to the products. A number before a formula indicates the number of molecules. Atoms shuffle around in a reaction, but they never disappear: The same number of atoms that enter a reaction remain at the reaction’s end.
Figure 5.7 Energy inputs and outputs in chemical reactions. 1 Endergonic reactions convert molecules with lower energy to molecules with higher energy, so they require a net energy input in order to proceed. 2 Exergonic reactions convert molecules with higher energy to molecules with lower energy, so they end with a net energy output.
Figure 5.8 Activation energy. Most reactions will not begin without an input of activation energy, which is shown here as a bump in an energy hill. In this example, the reactants have more energy than the products. Activation energy keeps this and other exergonic reactions from starting spontaneously.
Figure 5.9 ATP, the energy currency of cells.
Figure 5.9 ATP, the energy currency of cells.
Figure 5.9 ATP, the energy currency of cells.
Figure 5.10 An example of an active site. This one is in a hexokinase, an enzyme that phosphorylates glucose and other six-carbon sugars.
Figure 5.10 An example of an active site. This one is in a hexokinase, an enzyme that phosphorylates glucose and other six-carbon sugars.
Figure 5.10 An example of an active site. This one is in a hexokinase, an enzyme that phosphorylates glucose and other six-carbon sugars.
Figure 5.10 An example of an active site. This one is in a hexokinase, an enzyme that phosphorylates glucose and other six-carbon sugars.
Figure 5.10 An example of an active site. This one is in a hexokinase, an enzyme that phosphorylates glucose and other six-carbon sugars.
Figure 5.10 An example of an active site. This one is in a hexokinase, an enzyme that phosphorylates glucose and other six-carbon sugars.
Figure 5.11 An enzyme enhances the rate of a reaction by lowering its activation energy.
Figure 5.12 Enzymes and temperature. Tyrosinase is involved in the production of melanin, a black pigment in skin cells. The form of this enzyme in Siamese cats is inactive above about 30ーC (86ーF), so the warmer parts of the cat’s body end up with less melanin, and lighter fur.
Figure 5.13 Enzymes and pH. Left, how pH affects three enzymes. Right, carnivorous plants of the genus Nepenthes grow in nitrogen-poor habitats. They secrete acids and protein-digesting enzymes into a fluid–filled cup that consists of a modified leaf. The enzymes release nitrogen from insects that are attracted to odors from the fluid and then drown in it. One of these enzymes functions best at pH 2.6.