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CHAPTER
Microbial Metabolism
5

Learning Objectives Check Your Understanding

5-1 Define metabolism, and describe the Distinguish catabolism from anabolism.
fundamental differences between
anabolism and catabolism.
5-2 Identify the role of ATP as an intermediate How is ATP an intermediate between
between catabolism and anabolism. catabolism and anabolism?
5-3 Identify the components of an enzyme. What is a coenzyme?
5-4 Describe the mechanism of enzymatic Why is enzyme specificity important?
action.
5-5 List the factors that influence enzymatic What happens to an enzyme below its
activity. optimal temperature? Above its optimal
temperature?
5-6 Distinguish competitive and Why is feedback inhibition noncompetitive
noncompetitive inhibition. inhibition?
5-7 Define ribozyme. What is a ribozyme?
5-8 Explain the term oxidation-reduction. Why is glucose such an important
molecule for organisms?
5-9 List and provide examples of three types Outline the three ways that ATP is
of phosphorylation reactions that generate generated.
ATP.
5-10 Explain the overall function of metabolic What is the purpose of metabolic
pathways. pathways?
5-11 Describe the chemical reactions of What happens during the preparatory and
glycolysis. energy-conserving stages of glycolysis?
 5-12 Identify the functions of the pentose What is the value of the pentose phosphate
phosphate and Entner-Doudoroff and Entner-Doudoroff pathways if they
pathways. produce only one ATP molecule?
5-13 Explain the products of the Krebs cycle. What are the principal products of the
Krebs cycle?
5-14 Describe the chemiosmotic model for ATP How do carrier molecules function in the
generation. electron transport chain?
5-15 Compare and contrast aerobic and Compare the energy yield (ATP) of
anaerobic respiration. aerobic and anaerobic respiration.

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41
 5-16 Describe the chemical reactions of, and list List four compounds that can be made
some products of, fermentation. from pyruvic acid by an organism that uses
fermentation.
5-17 Describe how lipids and proteins undergo What are the end-products of lipid and
catabolism. protein catabolism?
5-18 Provide two examples of the use of On what biochemical basis are
biochemical tests to identify bacteria in the Pseudomonas and Escherichia
laboratory. differentiated?
5-19 Compare and contrast cyclic and noncyclic How is photosynthesis important to
photophosphorylation. catabolism?
5-20 Compare and contrast the light-dependent What is made during the light-dependent
and light-independent reactions of reactions?
photosynthesis.
5-21 Compare and contrast oxidative How are oxidative phosphorylation and
phosphorylation and photophosphorylation similar?
photophosphorylation.
5-22 Write a sentence to summarize energy Summarize how oxidation enables
production in cells. organisms to get energy from glucose,
sulfur, or sunlight.
5-23 Categorize the various nutritional patterns Almost all medically important
among organisms according to carbon microbes belong to which of the four
source and mechanisms of carbohydrate aforementioned groups?
catabolism and ATP generation.
5-24 Describe the major types of anabolism and Where do amino acids required for protein
their relationship to catabolism. synthesis come from?
5-25 Define amphibolic pathways. Summarize the integration of metabolic
pathways using peptidoglycan synthesis as
an example.

New in This Edition

• A new Big Picture feature, addressing metabolism, has been added.
Key concepts:
Enzymes facilitate metabolic reactions.
ATP is used by microbes and other cells to manage energy needs.
Catabolic reactions couple with ATP synthesis.
Anabolic reactions couple with ATP breakdown.
• The discussion of enzyme specificity has been revised.
• Figure 5.25, showing photophosphorylation, has been revised.
• The discussion of chemoheterotrophs has been revised.

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 Chapter Summary
Catabolic and Anabolic Reactions (pp. 110–111)
ASM 3.1: Bacteria and Archaea exhibit extensive, and often unique,
metabolic diversity (e.g. nitrogen fixation, methane production, anox-
ygenic photosynthesis).
ASM 3.3: The survival and growth of any microorganism in a given en-
vironment depend on its metabolic characteristics.
1. The sum of all chemical reactions within a living organism is known as metabolism.
2. Catabolism refers to chemical reactions that result in the breakdown of more complex
organic molecules into simpler substances. Catabolic reactions usually release energy.
3. Anabolism refers to chemical reactions in which simpler substances are combined to
form more complex molecules. Anabolic reactions usually require energy.
4. The energy of catabolic reactions is used to drive anabolic reactions.
5. The energy for chemical reactions is stored in ATP.

Enzymes (pp. 111–117)

1. Enzymes are proteins, produced by living cells, that catalyze chemical reactions by
lowering the activation energy.
2. Enzymes are generally globular proteins with characteristic three-dimensional shapes.
3. Enzymes are efficient, can operate at relatively low temperatures, and are subject to
various cellular controls.
4. When an enzyme and substrate combine, the substrate is transformed, and the enzyme is
recovered.
5. Enzymes are characterized by specificity, which is a function of their active sites.

Naming Enzymes (p. 113)

6. Enzyme names usually end in -ase.
7. The six classes of enzymes are defined on the basis of the types of reactions they
catalyze.

Enzyme Components (pp. 113–114)

8. Most enzymes are holoenzymes, consisting of a protein portion (apoenzyme) and a
nonprotein portion (cofactor).
9. The cofactor can be a metal ion (iron, copper, magnesium, manganese, zinc, calcium, or
cobalt) or a complex organic molecule known as a coenzyme (NAD+, NADP+, FMN,
FAD, or coenzyme A).

Factors Influencing Enzymatic Activity (pp. 114–116)

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 ASM 3.2: The interactions of microorganisms among themselves and
with their environment are determined by their metabolic abilities (e.g.,
quorum sensing, oxygen consumption, nitrogen transformations).

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 10. At high temperatures, enzymes undergo denaturation and lose their catalytic properties;
at low temperatures, the reaction rate decreases.
11. The pH at which enzymatic activity is maximal is known as the optimum pH.
12. Enzymatic activity increases as substrate concentration increases until the enzymes are
saturated.
13. Competitive inhibitors compete with the normal substrate for the active site of the
enzyme. Noncompetitive inhibitors act on other parts of the apoenzyme or on the
cofactor and decrease the enzyme’s ability to combine with the normal substrate.

Feedback Inhibition (pp. 116–117)

14. Feedback inhibition occurs when the end-product of a metabolic pathway inhibits an
enzyme’s activity near the start of the pathway.

Ribozymes (p. 117)

15. Ribozymes are enzymatic RNA molecules that cut and splice RNA in eukaryotic cells.

Energy Production (pp. 117–119)

Oxidation-Reduction Reactions (pp. 117–118)
1. Oxidation is the removal of one or more electrons from a substrate. Protons (H+) are
often removed with the electrons.
2. Reduction of a substrate refers to its gain of one or more electrons.
3. Each time a substance is oxidized, another is simultaneously reduced.
4. NAD+ is the oxidized form; NADH is the reduced form.
5. Glucose is a reduced molecule; energy is released during a cell’s oxidation of glucose.

The Generation of ATP (pp. 118–119)

6. Energy released during certain metabolic reactions can be trapped to form ATP from
ADP and i (phosphate). Addition of a i to a molecule is called phosphorylation.
7. During substrate-level phosphorylation, a high-energy from an intermediate in
catabolism is added to ADP.
8. During oxidative phosphorylation, energy is released as electrons are passed to a series of
electron acceptors (an electron transport chain) and finally to O2 or another inorganic
compound.
9. During photophosphorylation, energy from light is trapped by chlorophyll, and electrons
are passed through a series of electron acceptors. The electron transfer releases energy
used for the synthesis of ATP.

Metabolic Pathways of Energy Production (p. 119)

ASM 3.2: The interactions of microorganisms among themselves and

with their environment are determined by their metabolic abilities (e.g.,
quorum sensing, oxygen consumption, nitrogen transformations).

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 10. A series of enzymatically catalyzed chemical reactions called metabolic pathways store
energy in and release energy from organic molecules.

Carbohydrate Catabolism (pp. 119–131)

1. Most of a cell’s energy is produced from the oxidation of carbohydrates.
2. The two major types of glucose catabolism are respiration, in which glucose is
completely broken down, and fermentation, in which it is partially broken down.

Glycolysis (p. 121)

3. The most common pathway for the oxidation of glucose is glycolysis. Pyruvic acid is the
end-product.
4. Two ATP and two NADH molecules are produced from one glucose molecule.

Alternatives to Glycolysis (p. 121)

ASM 3.1: Bacteria and Archaea exhibit extensive, and often unique,
metabolic diversity (e.g., nitrogen fixation, methane production, anox-
ygenic photosynthesis).
5. The pentose phosphate pathway is used to metabolize five-carbon sugars; one ATP and
12 NADPH molecules are produced from one glucose molecule.
6. The Entner-Doudoroff pathway yields one ATP and two NADPH molecules from one
glucose molecule.

Cellular Respiration (pp. 121–127)

7. During respiration, organic molecules are oxidized. Energy is generated from the electron
transport chain.
8. In aerobic respiration, O2 functions as the final electron acceptor.
9. In anaerobic respiration, the final electron acceptor is usually an inorganic molecule other
than O2.
10. Decarboxylation of pyruvic acid produces one CO2 molecule and one acetyl group.
11. Two-carbon acetyl groups are oxidized in the Krebs cycle. Electrons are picked up by
NAD+ and FAD for the electron transport chain.
12. From one molecule of glucose, oxidation produces six molecules of NADH, two mole-
cules of FADH2, and two molecules of ATP.
13. Decarboxylation produces six molecules of CO2.
14. Electrons are brought to the electron transport chain by NADH.
15. The electron transport chain consists of carriers, including flavoproteins, cytochromes,
and ubiquinones.
16. Protons being pumped across the membrane generate a proton motive force as electrons
move through a series of acceptors or carriers.
17. Energy produced from movement of the protons back across the membrane is used by
ATP synthase to make ATP from ADP and .

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 18. In eukaryotes, electron carriers are located in the inner mitochondrial membrane; in
prokaryotes, electron carriers are in the plasma membrane.
19. In aerobic prokaryotes, 38 ATP molecules can be produced from complete oxidation of a
glucose molecule in glycolysis, the Krebs cycle, and the electron transport chain.
20. In eukaryotes, 36 ATP molecules are produced from complete oxidation of a glucose
molecule.
21. The total ATP yield is less than in aerobic respiration because only part of the Krebs
cycle operates under anaerobic conditions.

Fermentation (pp. 127–131)

ASM 3.2: The interactions of microorganisms among themselves and

with their environment are determined by their metabolic abilities (e.g.,
quorum sensing, oxygen consumption, nitrogen transformations).
22. Fermentation releases energy from sugars or other organic molecules by oxidation.
23. O2 is not required in fermentation.
24. Two ATP molecules are produced by substrate-level phosphorylation.
25. Electrons removed from the substrate reduce NAD+.
26. The final electron acceptor is an organic molecule.
27. In lactic acid fermentation, pyruvic acid is reduced by NADH to lactic acid.
28. In alcohol fermentation, acetaldehyde is reduced by NADH to produce ethanol.
29. Heterolactic fermenters can use the pentose phosphate pathway to produce lactic acid and
ethanol.

Lipid and Protein Catabolism (p. 131)

1. Lipases hydrolyze lipids into glycerol and fatty acids.
2. Fatty acids and other hydrocarbons are catabolized by beta-oxidation.
3. Catabolic products can be further broken down in glycolysis and the Krebs cycle.
4. Before amino acids can be catabolized, they must be converted to various substances that
enter the Krebs cycle.
5. Transamination, decarboxylation, and dehydrogenation reactions convert the amino acids
to be catabolized.

Biochemical Tests and Bacterial Identification (pp. 131–133)

1. Bacteria and yeast can be identified by detecting action of their enzymes.
2. Fermentation tests are used to determine whether an organism can ferment a carbohy-
drate to produce acid and gas.

Photosynthesis (pp. 133–135)

1. Photosynthesis is the conversion of light energy from the sun into chemical energy; the
chemical energy is used for carbon fixation.

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 The Light-Dependent Reactions: Photophosphorylation (pp. 134–135)
2. Chlorophyll a is used by green plants, algae, and cyanobacteria; it is found in thylakoid
membranes.
3. Electrons from chlorophyll pass through an electron transport chain, from which ATP is
produced by chemiosmosis.
4. Photosystems are made up of chlorophyll and other pigments packed into thylakoid
membranes.
5. In cyclic photophosphorylation, the electrons return to the chlorophyll.
6. In noncyclic photophosphorylation, the electrons are used to reduce NADP+. The elec-
trons from H2O or H2S replace those lost from chlorophyll.
7. When H2O is oxidized by green plants, algae, and cyanobacteria, O2 is produced; when
H2S is oxidized by the sulfur bacteria, S0 granules are produced.

The Light-Independent Reactions: The Calvin-Benson Cycle (p. 135)

8. CO2 is used to synthesize sugars in the Calvin-Benson cycle.

A Summary of Energy Production Mechanisms (pp. 135–136)

1. Sunlight is converted to chemical energy in oxidation-reduction reactions carried on by
phototrophs. Chemotrophs can use this chemical energy.
2. In oxidation-reduction reactions, energy is derived from the transfer of electrons.
3. To produce energy, a cell needs an electron donor (organic or inorganic), a system of
electron carriers, and a final electron acceptor (organic or inorganic).

Metabolic Diversity among Organisms (pp. 136–140)

ASM 3.1: Bacteria and Archaea exhibit extensive, and often unique,
metabolic diversity (e.g., nitrogen fixation, methane production, anox-
ygenic photosynthesis).
1. Photoautotrophs obtain energy by photophosphorylation and fix carbon from CO2 via the
Calvin-Benson cycle to synthesize organic compounds.
2. Cyanobacteria are oxygenic phototrophs. Green bacteria and purple bacteria are
anoxygenic phototrophs.
3. Photoheterotrophs use light as an energy source and an organic compound for their
carbon source and electron donor.
4. Chemoautotrophs use inorganic compounds as their energy source and carbon dioxide as
their carbon source.
5. Chemoheterotrophs use complex organic molecules as their carbon and energy sources.

Metabolic Pathways of Energy Use (pp. 140–142)

Polysaccharide Biosynthesis (pp. 140–141)
1. Glycogen is formed from ADPG.

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 2. UDPNAc is the starting material for the biosynthesis of peptidoglycan.

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Lipid Biosynthesis (p. 141)
3. Lipids are synthesized from fatty acids and glycerol.
4. Glycerol is derived from dihydroxyacetone phosphate, and fatty acids are built from
acetyl CoA.

Amino Acid and Protein Biosynthesis (pp. 141–142)

5. Amino acids are required for protein biosynthesis.
6. All amino acids can be synthesized either directly or indirectly from intermediates of
carbohydrate metabolism, particularly from the Krebs cycle.

Purine and Pyrimidine Biosynthesis (p. 142)

7. The sugars composing nucleotides are derived from either the pentose phosphate
pathway or the Entner-Doudoroff pathway.
8. Carbon and nitrogen atoms from certain amino acids form the backbones of the purines
and pyrimidines.

The Integration of Metabolism (pp. 142–143)

1. Anabolic and catabolic reactions are integrated through a group of common
intermediates.
2. Such integrated metabolic pathways are referred to as amphibolic pathways.

The Loop
Complete metabolic pathways are provided in Appendix A. The boxes in Chapter 1, Chapter
2, Chapter 11, Chapter 27, and Chapter 28 illustrate applications of microbial metabolism in
bioremediation and industry. Chapters 27 and 28 can be included with the study of Chapter 5
to provide students with applications of metabolism.

Answers
Figure Questions
Figure Question Answer
5.1 How does ATP provide the energy for Hydrolysis of ATP produces energy that
synthesis? can be used in another chemical reaction.
5.2 Why does a chemical reaction require Energy is needed to disrupt the stable
increased activation energy without an electronic configuration of the reactants.
enzyme as a biological catalyst?
5.3 How does the enzyme–substrate Changes the configuration of the reactants,
complex lower the activation energy of increasing collisions
the reaction?

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 5.4 Give an example of enzymatic The polymers of glucose (e.g., starch,
specificity. cellulose, dextran) have different bonding
between the glucose monomers, which can
only be hydrolyzed by a specific enzyme
(e.g., amylase, cellulase, dextranase).
5.5 How will this enzyme act at 25°C? It will act at 25°C and 45°C, but below its
At 45°C? At pH 7? optimum rate. It will be slower at 45°C
than at 25°C. It will act at its optimum rate
at pH 7.
5.6 When is denaturation irreversible? It is irreversible if the enzyme has lost its
solubility and coagulates.
5.7 How do competitive inhibitors operate Competitive inhibitors bind to the active
in comparison to noncompetitive site so more substrate is needed for the
inhibitors? reaction to occur. Noncompetitive
inhibitors bind to another site altering the
shape of the active site and the reaction
cannot occur.
5.8 Explain the differences between Competitive inhibition (see Fig. 5.7) is
competitive inhibition and feedback usually from an environmental chemical.
inhibition. Feedback inhibition is usually
noncompetitive inhibition (see Fig. 5.7).
5.9 How do oxidation and reduction differ? Oxidation is loss of electrons; reduction is
gaining electrons.
5.10 How do organisms use Oxidation reactions provide energy for
oxidation-reduction reactions? the cell; reduction reactions are needed to
accept the electrons from oxidation.
5.12 What is glycolysis? Oxidation of glucose to pyruvic acid
5.13 What are the products of the Krebs CO2, NADH + H+, and FADH2
cycle?
5.14 What are the functions of the electron To generate a proton motive force that
transport chain? can drive ATP synthase; reoxidize NADH
produced in glycolysis and the Krebs
cycle.
5.15 What is the proton motive force? Energy from the transfer of protons across
a membrane
5.16 Where does chemiosmosis occur in Inner mitochondrial membrane in
eukaryotes? In prokaryotes? eukaryotes; plasma membrane in
prokaryotes
5.17 How do aerobic and anaerobic The final electron acceptors are different.
respiration differ? The final electron acceptor in aerobic
respiration is O2.
5.18 During which phase of fermentation is During glycolysis
ATP generated?

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 5.19 What is the difference between Homolactic fermentation produces only
homolactic and heterolactic lactic acid. Heterolactic fermentation
fermentation? produces lactic acid and other products
such as CO2.
5.20 What is the role of lipases? Hydrolysis of lipids
5.21 What are the catabolic pathways through The electrons are transferred to NAD+ or
which high-energy electrons from all FAD, and then go to the electron transport
kinds of organic molecules flow on their chain.
energy-releasing pathways?

5.22 What is decarboxylation? Removal of the carboxyl (–COO) group

5.23 On what is the S. epidermidis growing? Peptone
5.24 What chemical reaction causes the Hydrolysis
release of H2S?
5.25 How are oxidative phosphorylation and Both use an electron transport chain to
photophosphorylation similar? generate ATP.
5.26 In the Calvin-Benson cycle, which mol- Glyceraldehyde 3-phosphate
ecule is used to synthesize sugars?
5.27 Are energy-generating reactions Oxidations
oxidations or reductions?
5.28 What is the basic difference between Their energy sources (chemical energy,
chemotrophs and phototrophs? light)
5.29 How are polysaccharides used in cells? Cell wall synthesis; energy storage
5.30 What is the primary use of lipids in Synthesizing cell membranes
cells?
5.31 What is the function of amino acids in Amino acids are used to make proteins.
cells?
5.32 What are the functions of nucleotides Nucleotides are used to make ATP, NAD+,
in a cell? FAD, DNA, and RNA.
5.33 What is the purpose of an amphibolic These pathways are used for oxidation of
pathway? substrates and synthesis of molecules.

Review
1. (a) is the Calvin-Benson cycle, (b) is glycolysis, and (c) is the Krebs cycle.
a. Glycerol is catabolized by pathway (b) as dihydroxyacetone phosphate; fatty acids by
pathway (c) as acetyl groups.
b. In pathway (c) at α-ketoglutaric acid
c. Glyceraldehyde-3-phosphate from the Calvin-Benson cycle enters glycolysis. Pyruvic
acid from glycolysis is decarboxylated to produce acetyl for the Krebs cycle.
d. In (a), between glucose and glyceraldehyde-3-phosphate

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 e. The conversion of pyruvic acid to acetyl, isocitric acid to α-ketoglutaric acid, and
α-ketoglutaric acid to succinyl CoA
f. By pathway (c) as acetyl groups
g. Uses Produces
Calvin-Benson cycle 6 NADPH
Glycolysis 2 NADH
Pyruvic acid → acetyl 1 NADH
Isocitric acid → α-ketoglutaric acid 1 NADH
α-ketoglutaric acid → succinyl CoA 1 NADH
Succinic acid → fumaric acid 1 FADH2
Malic acid → oxaloacetic acid 1 NADH
h. Dihydroxyacetone phosphate; acetyl; oxaloacetic acid; α-ketoglutaric acid
2.

3.

4. a. Oxidation-reduction: A coupled reaction in which one substance loses electrons and

another gains electrons.
b. The final electron acceptor in aerobic respiration is molecular oxygen; in anaerobic
respiration, it is another inorganic molecule.

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 c. In cyclic photophosphorylation, electrons are returned to chlorophyll. In noncyclic
photophosphorylation, chlorophyll receives electrons from hydrogen atoms.
5. a. Photophosphorylation
b. Oxidative phosphorylation
c. Substrate-level phosphorylation
6. Oxidation
7. a. CO2 d. Light g. Organic molecules
b. Light e. CO2 h. Organic molecules
c. Organic molecules f. Inorganic molecules
8. Protons are pumped from one side of the membrane to the others; transfer of protons
back across the membrane generates ATP. (a) Outer portion is acidic and (b) has a posi-
tive electrical charge. (c) Energy-conserving sites are the three loci where protons are
pumped out. (d) Kinetic energy is realized at ATP synthase.
9. NAD+ is needed to pick up more electrons. NADH is usually reoxidized in respiration.
NADH can be reoxidized in fermentation.
10. Chemoautotroph

Multiple Choice
1. a 6. b
2. d 7. b
3. b 8. a
4. c 9. c
5. c 10. b

Analysis
1. Streptococcus is only capable of fermentation, which yields two molecules of ATP for
each molecule of glucose consumed. Most of the energy that cells obtain from catabolism
is from respiration.
2. The rate at which an enzyme converts substrate to product is partly a function of initial
concentration of substrate. The more substrate molecules available, the more frequently
they access the active site of the enzyme. The reaction proceeds at a linear rate (black).
When the concentration of substrate is high enough that all enzyme molecules have their
active sites engaged, the reaction rate will remain constant. More substrate is needed
when a competitive inhibitor is present. When the enzyme becomes saturated with
competitive inhibitor, the reaction will completely stop (red).
3. Carbohydrate catabolism:
a. Oxidation of glucose (glycolysis, Krebs, aerobic ETC)
b. Following the Calvin-Benson cycle: oxidation of glucose (glycolysis, Krebs, aerobic
ETC)
c. Following the Calvin-Benson cycle: oxidation of glucose (glycolysis, Krebs, anaerobic
ETC)

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 Energy production: All three use chemiosmotic mechanisms. In addition to oxidative
phosphorylation, Spirulina and Ectothiorhodospira use photophosphorylation.
4. Glucose = 38 ATP
Triglyceride = 233 ATP. Glycerol is converted to PGAL and metabolized in glycolysis to
produce 2 ATP and 1 NADH. Six acetyl groups are produced from each of the 12-carbon
chains by beta-oxidation. Each acetyl enters the Krebs cycle to yield 1 ATP, 3 NADH,
and 1 FADH.
5. Two electrons removed from As3+ are picked up by NAD+ for use in the electron trans-
port chain. Thiobacillus could be used to remove arsenic from industrial wastewater and
groundwater.

Clinical Applications and Evaluation

1. X factor is necessary to synthesize cytochromes. V factor is used as an electron acceptor
in oxidation reactions.
2. The drug ddC is missing an O atom on C3, so it cannot be joined to the phosphate group
of another nucleotide.
3. Live bacteria or whole bacterial cells are not being injected. Enzymes are specific for
their substrates, so streptokinase will react only with its substrate, fibrin.

Case Study: The Pasteur Effect

Background
In 1861, Louis Pasteur observed that when yeasts grow in a sugar-and-protein medium com-
pletely free of air, they ferment vigorously, and for every gram of yeast that forms, 60 to 80
grams of sugar disappear. If the experiment is carried out in the presence of air, for 1 gram of
yeast that forms, only 4 to 10 grams of sugar are removed. The yeasts again ferment if trans-
ferred to a sugar-containing medium absent air.
When the experiment is repeated with a protein medium, the yeasts grow only in the
presence of oxygen. Pasteur concluded that the yeasts can take oxygen from air, and in the
absence of air, the yeasts take oxygen from the sugar.
Pasteur applied quantitative methods to his studies of fermentation and was the first to
report on organisms that could live and reproduce in the absence of oxygen. His conclusion
was, however, incorrect. These different behaviors of yeasts are known today as the “Pasteur
effect.”

Questions
1. Explain the three yeast behaviors based on modern concepts of microbial metabolism.
2. What was incorrect about Pasteur’s conclusion?

The Solution
1. The yeasts are able to grow anaerobically if a fermentable sugar is available. Fermenta-
tion consumes more sugar than respiration to produce the same amount of energy.
2. Pasteur assumed yeasts were taking oxygen from the sugar.

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