Biochemistry 1st Edition Miesfeld Test Bank

Biochemistry 1st Edition Miesfeld Test
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Chapter 10: The Citrate Cycle
Learning Objectives
10.1 The Citrate Cycle Captures Energy Using Redox 10.2.d. Hypothesize why the activity of pyruvate
Reactions dehydrogenase is so tightly controlled by the cell.
10.1.a. Describe the role of NAD+ and FAD in the 10.3 Enzymatic Reactions of the Citrate Cycle
citrate cycle.
10.3.a. Classify the eight reactions of the citrate cycle as
10.1.b. State the net reaction of the citrate cycle. either exergonic or endergonic.
10.1.c. List the functions of the key enzymes of the 10.3.b. Identify the steps of the citrate cycle in which
citrate cycle. NADH, FADH2, CO2, and GTP are produced.
10.1.d. Explain how change in free energy can be found 10.4 Regulation of the Citrate Cycle
from differences in reduction potential.
10.4.a. Hypothesize whether the citrate cycle would be
10.2 Pyruvate Dehydrogenase Converts Pyruvate to activated or inhibited by high concentrations of AMP, ADP,
Acetyl-CoA or ATP.
10.2.a. Explain the importance of the vitamins niacin, 10.4.b. Describe the effect of high concentrations of NADH
riboflavin, pantothenic acid, and thiamine to the upon the citrate cycle.
citrate cycle.
10.5 Metabolism of Citrate Cycle Intermediates
10.2.b. Classify the organic reaction that converts pyruvate
into acetyl-CoA. 10.5.a. List the anaplerotic reactions of the citrate cycle.
10.2.c. Summarize the effect of arsenic on pyruvate 10.5.b. Describe the potential fates of oxaloacetate,
dehydrogenase. a-ketoglutarate, and succinyl-CoA in the cell.
Chapter 10: The Citrate Cycle
MULTIPLE CHOICE
1. Which molecules function as electron acceptors in the citrate cycle?

a. NAD+, FAD
b. NADH, FADH2
c. GDP, ADP
d. GTP, ATP
ANS: A DIF: Easy REF: 10.1
OBJ: 10.1.a. Describe the role of NAD+ and FAD in the citrate cycle.
MSC: Remembering
2. In two turns of the citrate cycle, how many electrons are transferred from the citrate cycle
intermediates to NAD+ and FAD?
a. 4
b. 8
c. 12
d. 16
ANS: D DIF: Easy REF: 10.1
MSC: Applying
3. The primary function of NAD+ in the citrate cycle is that it

a. functions as an electron donor.
b. is oxidized to produce GTP.
c. acts as an electron acceptor.
d. phosphorylates ADP.
ANS: C DIF: Easy REF: 10.1
MSC: Remembering
4. Regeneration of NAD+ and FAD inside the mitochondrial matrix is required because
a. anabolic reactions generally require them.
b. they produce GDP through the citrate cycle.
c. they transport pyruvate through the matrix.
d. they maintain flux through the citrate cycle.
ANS: D DIF: Medium REF: 10.1
MSC: Analyzing
5. Where do citrate cycle reactions in eukaryotic cells take place?

a. cytosol
b. mitochondrial matrix
c. endoplasmic reticulum
d. nucleus
ANS: B DIF: Easy REF: 10.1
OBJ: 10.1.b. State the net reaction of the citrate cycle. MSC: Remembering
1
6. The primary function of the citrate cycle is to oxidize
a. glucose.
b. pyruvate.
c. acetyl-CoA.
d. citrate.
7. How many ATP are produced from two turns of the citrate cycle?
a. 9
b. 10
c. 18
d. 20
OBJ: 10.1.b. State the net reaction of the citrate cycle. MSC: Applying
8. Which of the following is a reactant in the net reaction of the citrate cycle?
a. CO2
b. H2 O
c. GTP
d. CoA
9. Which of the following is a product of the net reaction of the citrate cycle?
a. FAD
b. H2 O
c. H+
d. NAD+
10. Which molecule in the net reaction of the citrate cycle contributes to the inhibition of
pyruvate dehydrogenase?
a. FAD
b. H2 O
c. H+
d. NADH
11. Which enzyme regulates the flux of acetyl-CoA through the citrate cycle?
a. pyruvate dehydrogenase
b. citrate synthase
c. isocitrate dehydrogenase
d. -ketoglutarate dehydrogenase
OBJ: 10.1.c. List the functions of the key enzymes of the citrate cycle.
MSC: Remembering
2
12. Which enzyme in the citrate cycle is activated by CoA?
b. citrate synthase
MSC: Applying
13. Which enzyme of the citrate cycle catalyzes the oxidative decarboxylation reaction that
produces CO2 , NADH, and succinyl-CoA?
b. citrate synthase
MSC: Remembering
14. The poison compound 1080 converts fluoroacetate to fluorocitrate. Which enzyme in the
citrate cycle is inhibited by this poison?
a. aconitase
b. citrate synthase
ANS: A DIF: Difficult REF: 10.1
MSC: Applying
15. Which enzyme in the citrate cycle produces NADH?

a. aconitase
b. citrate synthase
d. fumarase
MSC: Remembering
16. Which enzyme requires CoASH to produce acetyl-CoA?

b. citrate synthase
MSC: Remembering
3
17. Calculate the E° of a coupled redox reaction with O2 and ferredoxin (Fe2+) using the table
below.
a. 1.25
b. 0.39
c. 0.39
d. 1.25
ANS: D DIF: Difficult REF: 10.1
OBJ: 10.1.d. Explain how change in free energy can be found from differences in reduction
potential. MSC: Applying
4
18. Identify the strongest oxidant in the table below.
a. O2
b. oxaloacetate
c. pyruvate
d. ferredoxin
potential. MSC: Understanding
5
19. Identify the strongest reductant in the table below.
a. O2
b. oxaloacetate
c. pyruvate
d. ferredoxin
6
20. Calculate the G° of a redox reaction of pyruvate and hydrogen under standard conditions
using the table below.
a. 18.33 kJ/mol
b. 36.66 kJ/mol
c. 54.99 kJ/mol
d. 73.32 kJ/mol
ANS: B DIF: Medium REF: 10.1
21. In linked metabolic pathways, the oxidants in subsequent reactions must

a. result in negative E° values at each reaction step.
b. result in positive G° values at each reaction step.
c. have progressively lower standard reduction potentials.
d. have progressively higher standard reduction potentials.
22. Coenzyme A is derived from which of the following vitamins?

a. thiamine
b. pantothenic acid
c. riboflavin
d. niacin
OBJ: 10.2.a. Explain the importance of the vitamins niacin, riboflavin, pantothenic acid, and
thiamine to the citrate cycle. MSC: Remembering
7
23. Which vitamin is the precursor to the coenzyme that functions as a reductant in the pyruvate
dehydrogenase complex in the final step of the reaction?
a. thiamine
b. pantothenic acid
c. riboflavin
d. niacin
ANS: C DIF: Medium REF: 10.2
24. Pantothenic acid is essential for life because it is the vitamin precursor to the molecule that
a. provides a reactive disulfide that can participate in redox reactions within the enzyme
active site of pyruvate dehydrogenase.
b. can accept one or two electrons in redox reactions in the cell.
c. is involved in at least 200 redox reactions in the cell.
d. is a cofactor in the biosynthetic pathways that produce fatty acids, acetylcholine,
heme, and cholesterol.
thiamine to the citrate cycle. MSC: Analyzing
25. Thiamine pyrophosphate functions as a coenzyme in which reactions in the citrate cycle?
a. pyruvate dehydrogenase and succinate dehydrogenase
b. pyruvate dehydrogenase and -ketoglutarate dehydrogenase
c. malate dehydrogenase and succinate dehydrogenase
d. malate dehydrogenase and -ketoglutarate dehydrogenase
ANS: B DIF: Difficult REF: 10.2
26. The disease beriberi is a result of which vitamin deficiency?

a. thiamine
b. pantothenic acid
c. riboflavin
d. niacin
27. Identify the coenzyme that provides a reactive disulfide that participates in the redox reaction
in the active site of pyruvate dehydrogenase.
a. NAD+
b. coenzyme A
c. lipoamide
d. thiamine pyrophosphate
thiamine to the citrate cycle. MSC: Understanding
8
28. Classify the reaction that occurs at step 5 in the reaction schematic of the pyruvate
dehydrogenase reaction below.
a. isomerization
b. addition
c. oxidation reduction
d. decarboxylation
OBJ: 10.2.b. Classify the organic reaction that converts pyruvate into acetyl-CoA.
MSC: Analyzing
a. isomerization
b. addition
d. decarboxylation
MSC: Analyzing
9
a. isomerization
b. addition
d. decarboxylation
MSC: Analyzing
31. Identify the E1 subunit in the reaction schematic of the pyruvate dehydrogenase reaction
below.
b. dihydrolipoyl dehydrogenase
c. dihydrolipopyl acetyltransferase
d. flavin adenine dinucleotide
MSC: Understanding
10
32. Identify the E2 subunit in the reaction schematic of the pyruvate dehydrogenase reaction
below.
b. dihydrolipoyl dehydrogenase
MSC: Understanding
33. What is the purpose of the first 3 steps in the pyruvate dehydrogenase reaction?
a. regenerate the oxidized form of lipoamide
b. form NADH
c. transfer electrons
d. form acetyl-CoA
MSC: Applying
11
34. Which coenzyme in the citrate cycle is affected by arsenic?
a. coenzyme A
b. thiamine pyrophosphate
OBJ: 10.2.c. Summarize the effect of arsenic on pyruvate dehydrogenase.
MSC: Remembering
35. Which of the following is the cause of the irreversible blockage of the catalytic activity of
lipoamide-containing enzymes?
a. cheilosis
b. pellagra
c. beriberi
d. arsenic poisoning
MSC: Understanding
36. A patient seeks medical attention for ulcerous skin lesions. The patient is diagnosed with
a. arsenic exposure.
b. a deficiency in vitamin B3.
c. beriberi.
d. cheilosis.
ANS: A DIF: Medium REF: 10.2
MSC: Applying
37. Which two enzymes in the citrate cycle are affected by arsenic poisoning?
a. pyruvate dehydrogenase and succinate dehydrogenase
b. pyruvate dehydrogenase and -ketoglutarate dehydrogenase
c. malate dehydrogenase and succinate dehydrogenase
d. malate dehydrogenase and -ketoglutarate dehydrogenase
MSC: Remembering
38. Arsenite affects the lipoamide coenzymes of the pyruvate dehydrogenase reaction by
a. acting as a competitive inhibitor.
b. covalently modifying the coenzyme.
c. being a noncompetitive inhibitor.
d. modifying the coenzyme through electrostatic interactions.
MSC: Understanding
12
39. If acetyl-CoA is not metabolized by the citrate cycle, the molecule in the cell
a. undergoes fatty acid metabolism.
b. is transported across the cell membrane.
c. is used to synthesize amino acids.
d. is used during glycolysis.
OBJ: 10.2.d. Hypothesize why the activity of pyruvate dehydrogenase is so tightly controlled
by the cell. MSC: Analyzing
40. How would an increase in Ca2+ be expected to affect the pyruvate dehydrogenase reaction?
a. The pyruvate dehydrogenase kinase enzyme activity would increase, resulting in an
inhibition of pyruvate dehydrogenase activity.
b. The last step of the pyruvate dehydrogenase reaction is blocked, resulting in a
decrease in activity.
c. The E1 subunit is phosphorylated by pyruvate dehydrogenase kinase, and the
catalytic activity of pyruvate dehydrogenase decreases.
d. The pyruvate dehydrogenase phosphatase-1 enzyme would increase, resulting in
pyruvate dehydrogenase activation at an accelerated rate.
by the cell. MSC: Applying
41. How is the pyruvate dehydrogenase reaction regulated?

a. pH and enzyme conformation
b. pH and the protonation state of the active site
c. allosteric control and covalent modification
d. product inhibition
by the cell. MSC: Understanding
42. How would a high NADH to NAD+ ratio be expected to affect the pyruvate dehydrogenase
reaction?
increase in pyruvate dehydrogenase activity.
b. The last step of the pyruvate dehydrogenase reaction is blocked, resulting in a
c. The E1 subunit is phosphorylated by pyruvate dehydrogenase kinase, and the
catalytic activity of pyruvate dehydrogenase decreases.
13
43. How would an increased level of acetyl-CoA be expected to affect the pyruvate dehydrogenase
reaction?
inhibition of pyruvate dehydrogenase activity.
b. The last step of the pyruvate dehydrogenase reaction would be blocked, resulting in a
c. The E1 subunit would be phosphorylated by pyruvate dehydrogenase kinase, and the
catalytic activity of pyruvate dehydrogenase would decrease.
44. The reaction catalyzed by __________is the most endergonic reaction in the citrate cycle.
a. fumarase
b. succinate dehydrogenase
c. malate dehydrogenase
d. aconitase
OBJ: 10.3.a. Classify the eight reactions of the citrate cycle as either exergonic or
endergonic.
MSC: Remembering
45. The reaction catalyzed by __________ is the most exergonic reaction in the citrate cycle.
a. citrate synthase
b. fumarase
endergonic.
MSC: Remembering
46. Why is the G° of the condensation of oxaloacetate and acetyl-CoA highly favorable?
a. The addition of inorganic phosphate provides energy, resulting in the highly
favorable nature of this reaction.
b. Allosteric regulations of the reaction cause a release of energy, making the reaction
thermodynamically favorable.
c. The iron-sulfur cluster in the enzyme reduces the activation energy of the reaction,
resulting in the favorable G°.
d. The hydrolysis of the thioester bond in citryl-CoA results in the highly exergonic
reaction.
endergonic.
MSC: Understanding
14
47. The reaction catalyzed by __________ is likely to be reversible under cellular conditions
according to the G°.
a. malate dehydrogenase
b. citrate synthase
c. succinate dehydrogenase
endergonic.
MSC: Applying
48. According to the G°, which of the following exergonic reactions is most likely irreversible
under normal cellular conditions and is considered to be the rate-limiting step of the citrate
cycle?
a. citrate synthase
b. fumarase
endergonic.
MSC: Remembering
15
49. Which reactions in the citrate cycle produce CO2 ?
a. 1 and 2
b. 2 and 3
c. 3 and 4
d. 4 and 5
OBJ: 10.3.b. Identify the steps of the citrate cycle in which NADH, FADH2, CO2, and GTP
are produced. MSC: Understanding
16
50. Which reactions in the citrate cycle produce NADH?
a. 1, 2, and 4
b. 3, 4, and 8
c. 3, 6, and 7
d. 5, 6, and 8
17
51. Which reaction in the citrate cycle produces GTP?
a. 3
b. 4
c. 5
d. 6
18
52. Which reaction in the citrate cycle produces FADH2 ?
a. 3
b. 4
c. 5
d. 6
19
53. Which reaction in the citrate cycle produces NADH?
a. 4
b. 5
c. 6
d. 7
20
54. Which reaction in the citrate cycle produces CO2 ?
a. 1
b. 2
c. 3
d. 5
55. A high concentration of which molecule would inhibit citrate synthase in the citrate cycle?
a. AMP
b. ADP
c. NAD+
d. A T P
OBJ: 10.4.a. Hypothesize whether the citrate cycle would be activated or inhibited by high
concentrations of AMP, ADP, or ATP. MSC: Understanding
56. What enzyme in the citrate cycle is activated by high concentrations of AMP?
a. isocitrate dehydrogenase
b. -ketoglutarate dehydrogenase
c. citrate synthase
d. succinyl-CoA synthetase
21
57. An in vitro study shows that isocitrate dehydrogenase is activated in the citrate cycle. What is
a possible explanation for the activation?
a. high levels of ATP
b. low levels of ATP
c. high levels of NADH
d. low levels of AMP
concentrations of AMP, ADP, or ATP. MSC: Applying
58. An in vitro study shows that -ketoglutarate dehydrogenase is inhibited in the citrate cycle.
What is a possible explanation for this inhibition?
a. high levels of ATP
b. low levels of Ca2+
c. low levels of NADH
d. high levels of ADP
59. High levels of ATP would result in the inhibition of which enzyme in the citrate cycle?
a. succinate dehydrogenase
b. isocitrate dehydrogenase
c. malate dehydrogenase
d. fumarase
60. In the citrate cycle, a high concentration of NADH would result in

a. activation of citrate synthase.
b. inhibition of -ketoglutarate dehydrogenase.
c. inhibition of fumarase.
d. activation of -ketoglutarate dehydrogenase.
OBJ: 10.4.b. Describe the effect of high concentrations of NADH on the citrate cycle.
MSC: Applying
61. An in vitro study shows that citrate synthase is inhibited in the citrate cycle. What is a possible
explanation for this inhibition?
a. high levels of ADP
b. low levels of succinyl-CoA
c. high levels of NADH
d. high levels of AMP
MSC: Applying
22
62. A high NADH to NAD+ ratio would inhibit which enzyme in the citrate cycle?
a. succinate dehydrogenase
b. succinyl-CoA synthetase
c. aconitase
d. isocitrate dehydrogenase
MSC: Applying
63. The regulatory mechanism in the citrate cycle involving the NADH to NAD+ ratio is
considered to be an example of regulation by
a. pH and protonation state.
b. product inhibition.
c. covalent modification.
d. pH and enzyme conformation.
MSC: Applying
64. A low NADH to NAD+ ratio would activate which enzyme in the citrate cycle?
a. succinyl-CoA synthetase
b. fumarase
c. citrate synthase
d. succinate dehydrogenase
MSC: Applying
65. The citrate cycle is considered to be a(n) __________ pathway.

a. anabolic
b. catabolic
c. anaplerotic
d. amphibolic
OBJ: 10.5.a. List the anaplerotic reactions of the citrate cycle.
MSC: Remembering
66. Which anaplerotic reaction balances the input of oxaloacetate with acetyl-CoA in the citrate
cycle by converting pyruvate into oxaloacetate?
a. pyruvate carboxylase
b. malate dehydrogenase
c. malic enzyme
d. pyruvate kinase
MSC: Understanding
23
67. The anaplerotic reaction catalyzed by pyruvate carboxylase requires which coenzyme?
a. niacin
b. biotin
c. riboflavin
d. thiamine
MSC: Remembering
68. When the citrate cycle is inhibited, which two metabolites are exported to the cytosol for
fatty acid and cholesterol synthesis?
a. malate and succinyl-CoA
b. succinyl-CoA and -ketoglutarate
c. -ketoglutarate and citrate
d. citrate and malate
MSC: Understanding
69. Which citrate cycle intermediate is siphoned off the citrate cycle during starvation?
a. succinyl-CoA
b. malate
c. -ketoglutarate
d. fumarate
ANS: B DIF: Difficult REF: 10.5
MSC: Applying
70. Which anaplerotic reactions do plants, yeast, and bacteria use to generate oxaloacetate?
a. pyruvate carboxylase
b. malic enzyme
c. phosphoenolpyruvate carboxylase
d. malate dehydrogenase
MSC: Remembering
71. Which citrate cycle metabolite is used as a precursor for heme biosynthesis?
a. succinyl Co-A
b. oxaloacetate
c. -ketoglutarate
d. malate
OBJ: 10.5.b. Describe the potential fates of oxaloacetate, alpha-ketoglutarate,
and succinyl-CoA in the cell. MSC: Understanding
24
72. What is the fate of oxaloacetate when it is not used in the citrate cycle?
a. cholesterol synthesis
b. heme synthesis
c. amino acid synthesis
d. gluconeogenesis
and succinyl-CoA in the cell. MSC: Applying
73. Predict the fate of -ketoglutarate when it is not used in the citrate cycle.
b. heme synthesis
c. gluconeogenesis
d. amino acid synthesis
74. Which citrate cycle intermediate is also used in gluconeogenesis?

a. oxaloacetate
b. -ketoglutarate
c. fumarate
d. succinate
and succinyl-CoA in the cell. MSC: Analyzing
75. Predict the fate of succinyl-CoA in the cell when it is not in the citrate cycle.
b. heme synthesis
c. gluconeogenesis
d. amino acid synthesis
SHORT ANSWER
1. Describe the fate of NADH and FADH2 produced in the citrate cycle.
ANS:
NADH and FADH2 enter the electron transport system, where they are oxidized to NAD+ and
FAD. They produce ATP by the process of oxidative phosphorylation.
DIF: Medium REF: 10.1

MSC: Understanding
25
2. Compare and contrast the functions of NAD+ and FAD in the citrate cycle.
ANS:
Both NAD+ and FAD act as coenzymes. They accept electrons from the citrate cycle
intermediates and are oxidized in the electron transport chain. The citrate cycle requires three
NAD+ molecules, which accept a total of six electrons. In contrast, the cycle only requires one
FAD molecule, which accepts two electrons.

MSC: Analyzing
3. Use the overall net reaction of the citrate cycle to explain why excess NADH inhibits the
pyruvate dehydrogenase reaction.
ANS:
NADH is a product in the balanced citrate cycle reaction. The pyruvate dehydrogenase
reaction produces acetyl-CoA, which is a reactant in the balanced citrate cycle. When the cell
has excess NADH, there is no reason to produce more. The pyruvate dehydrogenase reaction
is inhibited so that the reactant acetyl-CO is diverted to fatty acid synthesis and more NADH
is not produced.
DIF: Difficult REF: 10.1

4. What two features of the citrate cycle make it unique compared with linear metabolic
pathways?
ANS:
Oxaloacetate is both the substrate for the first reaction and the last reaction, unlike linear
metabolic pathways. Because of this, if just one citrate cycle intermediate is added to the cells,
the concentrations of all the intermediates increase. Additionally, the enzymes pyruvate
dehydrogenase and pyruvate carboxylase control the flow of acetyl-CoA and oxaloacetate into
the citrate cycle.

MSC: Analyzing
26
5. Use the figure below to answer the following questions.
A. The electrochemical cell shown here is measuring the reduction potential of Fe2+/Fe3+ using
a reference hydrogen half reaction. Write each half reaction on the figure and show the flow
of electrons.
B. Do these oxidants have a higher or lower affinity for electrons compared with H+? Explain
how you know this using information from the experiment.
ANS:
A. The reference hydrogen half reaction should be written on the left side of the cell with the
electrons flowing from the left to the right. The iron half reaction should be on the right side
of the cell.
B. These oxidants have a higher affinity for electrons than H+ because the standard reduction
potential is greater than 0 (0.77 V).

27
6. Using the table below, calculate G° and determine if the conversion from malate to
oxaloacetate is favorable under standard biochemical conditions.
Malate + NAD+  Oxaloacetate + H+ + NADH
ANS:
Calculate the E for the coupled redox reaction.
E = –0.17 – (–0.32) = +0.15
Then, use this value to determine Gibbs free energy.

G° = –nFE°
G° = –(2)(96.48 kJ/V mol)(+0.15 V)

G° = –28.94 kJ/mol
This calculation shows that the conversion from malate to oxaloacetate is favorable because
G° is less than 0 under standard biochemical conditions.

7. Explain what redox reaction E° values mean regarding spontaneity. How does the
spontaneity affect the arrangement of multiple redox reactions in a linked metabolic pathway?
ANS:
Redox reactions with positive E° values proceed spontaneously, whereas redox reactions with
negative E° values do not proceed spontaneously. In linked metabolic pathways, the oxidants
in subsequent reactions must have progressively more positive standard reduction potentials
than in the previous reactions.

potential. MSC: Understanding | Applying
28
8. Corn-rich diets in Europe in the 1700s resulted in the disease pellagra. Though Mexico also
had a corn-rich diet at the time, this disease was rare there. Propose a reason for this
observation.
ANS:
Pellagra is the result of a niacin deficiency. Niacin is the precursor to NAD+ and NADP+,
which are needed for approximately 200 redox reactions in the cell, as well as the citrate
cycle. Niacin is present in corn but is bound to a protein that greatly reduces the ability of the
vitamin to be absorbed by the small intestine. Unlike in Europe, in Mexico the corn was
soaked in a lime solution (calcium oxide), which released niacin from the protein when the
corn was heated. Therefore, niacin deficiency was rare in Mexico.

thiamine to the citrate cycle. MSC: Evaluating
9. Coenzyme A does not readily cross the cell membrane. However, coenzyme A functions as an
acyl carrier in the citrate cycle in the mitochondrial matrix. Explain how coenzyme A crosses
the cell membrane to participate in the citrate cycle.
ANS:
Coenzyme A is degraded in the gut to pantothenic acid. Pantothenic acid is absorbed and
transported through the circulatory system to various tissues, where it is transported across the
cell membrane. Once inside the cell it is converted back to coenzyme A by several
phosphorylation reactions and reactions that require ASTP, cysteine, and cytidine
triphosphate.

10. Explain why riboflavin is critical to the citrate cycle.
ANS:
Riboflavin is the precursor to flavin adenine dinucleotide (FAD). FAD is a coenzyme in the
pyruvate dehydrogenase complex, functioning as a reductant. It is also covalently bound to the
enzyme succinate dehydrogenase and participates in the conversion of succinate to fumarate.

29
11. Outline the five reaction steps of the conversion from pyruvate to acetyl-CoA.
ANS:
Step 1: Pyruvate dehydrogenase catalyzes a decarboxylation reaction once it binds pyruvate,
releasing carbon dioxide. This forms hydroxyethyl-TPP.
Step 2: Hydroxyethyl-TPP reacts with the disulfide group of the lipoamide moiety on
dihydrolipoyl acetyltransferase, generating acetyl-dihydrolipoamide.
Step 3: Dihydrolipoyl transacetylase catalyzes the transfer of an acetyl group to CoA to yield
acetyl-CoA.
Step 4: Dihydrolipoyl dehydrogenase oxidizes lipoic acid to the disulfide form.
Step 5: An electron transfer from dihydrolipoyl dehydrogenase-FADH2 regenerates NADH.

MSC: Analyzing
12. Compare the two roles of lipoic acid in the pyruvate dehydrogenase reaction.
ANS:
Lipoic acid provides a reactive disulfide that participates in redox reactions at the enzyme
active site. Lipoic acid forms the lipoamide that participates in the transfer of the acetyl
group.

MSC: Analyzing
13. Explain how arsenic affects the pyruvate dehydrogenase reaction.
ANS:
Arsenite covalently modifies lipoamide coenzymes in the pyruvate dehydrogenase complex.
For example, the arsenite binds with the sulfide groups of dihydrolipoyl acetyl transferase.
This results in the oxidized form of the lipoamide that cannot be regenerated.

MSC: Understanding
14. You have a patient who has been traveling through India and Bangladesh who is presenting
with ulcerous skin lesions. What could cause this issue and what is your recommendation?
ANS:
The symptom plus the travel locales are indicative of arsenic poisoning. The patient should
have his or her water tested for arsenic and avoid drinking from the water supply because it
could be contaminated. Arsenic is also present in some paints, so the patient should avoid
paints as well.

MSC: Applying
30
15. You exercise vigorously for 30 minutes. Which chemical compounds would you expect to be
elevated that would affect the regulation of pyruvate dehydrogenase? State the substances and
explain how they would affect the regulation.
ANS:
Muscle contraction results in an increase in calcium ions as well as an increased demand for
ATP. The NADH to NAD+ ratio is also low when cells are active metabolically. These
chemicals shift the metabolic flux toward catabolic pathways, so they would activate pyruvate
dehydrogenase to produce acetyl-CoA, which would produce ATP through the citrate cycle.
These molecules function as signals to turn on the oxidative enzymes to produce energy.

16. Compare the two ways the pyruvate dehydrogenase reaction is controlled by the cell.
ANS:
Pyruvate dehydrogenase is regulated by allotter control and covalent modification. The
allosteric control includes NADH to NAD+ ratio and CoA to acetyl-CoA ratio. When NADH
to NAD+ ratio is high, NADH competes with NAD+ for binding with dihydrolipoyl
dehydrogenase, preventing the reoxidation of NADH in the last step of the reaction. When
acetyl-CoA levels are high, acetyl CoA competes with CoA for binding to dihydrolipoyl
acetyltransferase, blocking pyruvate decarboxylation. Covalent modification includes the
phosphorylation of the pyruvate dehydrogenase enzyme catalyzed by pyruvate dehydrogenase
kinase. This covalent modification deactivates the pyruvate dehydrogenase enzyme.

by the cell. MSC: Analyzing
17. The G° of the conversion from malate to oxaloacetate in the last reaction of the citrate
cycle is very large, indicating this reaction is not thermodynamically favorable. Propose an
explanation for how this reaction can proceed in the forward direction despite the very
positive G° value.
ANS:
The oxaloacetate concentrations are kept very low in the cell by the conversion to citrate in
the first reaction, which is strongly exergonic. This allows the reaction to proceed in the
forward direction even though it is endergonic.

endergonic.
MSC: Evaluating
31
18. Briefly describe the eight reactions from the citrate cycle, including the identity of the organic
reactions and the energetic products.
ANS:
In the first reaction, oxaloacetate undergoes a condensation reaction with acetyl-CoA to form
citrate. Citrate then undergoes an isomerization reaction to form isocitrate, which undergoes
an oxidative decarboxylation reaction to form -ketoglutarate. -Ketoglutarate undergoes
another decarboxylation reaction to form succinyl-CoA. During each of these decarboxylation
reactions, CO2 is released and an NADH molecule is produced. The thiol bond from
succinyl-CoA is cleaved, producing GTP via a substrate level phosphorylation. Succinate
undergoes to redox reaction, producing fumarate and an FADH2 molecule. Fumarate undergoes
a hydration reaction to form malate, and malate undergoes a redox reaction to form
oxaloacetate and the final NADH molecule.

19. ATP regulates the citrate cycle but is not found as a direct product of any of the reactions.
Explain how ATP regulates the cycle and identify the enzymes that ATP regulates.
ANS:
ATP is an example of feedback inhibition. Low levels of ATP in the cell signal that the cell
needs more energy, and the citrate cycle is activated. Conversely, high levels of ATP in the
cell signal that no more is needed, and the citrate cycle is inhibited. The three enzymes in the
citrate cycle that ATP regulates are citrate synthase, isocitrate dehydrogenase, and
-ketoglutarate dehydrogenase.

20. Hypothesize how high concentrations of the following would either inhibit or activate the
specific enzymes of the citrate cycle and the citrate cycle as a whole.
A. AMP
B. ATP
C. ADP
ANS:
A. High levels of AMP would activate -ketoglutarate dehydrogenase, resulting in the
activation of the citrate cycle.
B. High levels of ATP inhibit the citrate cycle by inhibiting citrate synthase, isocitrate
dehydrogenase, and -ketoglutarate dehydrogenase, resulting in the inhibition of the citrate
cycle.
C. High levels of ADP would activate isocitrate dehydrogenase and citrate synthase, resulting
in the activation of the citrate cycle.

concentrations of AMP, ADP, or ATP. MSC: Evaluating
32
21. Explain the effect a high concentration of NADH has on the citrate cycle.
ANS:
High NADH implies that the cell does not need energy, resulting in the inhibition of the
citrate cycle. Specifically, high NADH concentrations inhibit the citrate cycle by inhibiting
citrate synthase, isocitrate dehydrogenase, and -ketoglutarate dehydrogenase.
DIF: Easy REF: 10.4

MSC: Understanding
22. Predict what happens to citrate in a cell when ATP and NADH concentrations are high.
ANS:
The citrate cycle is inhibited under these conditions, so citrate is exported from the
mitochondria to the cytosol. In the cytosol, citrate is cleaved by citrate lyase, releasing
acetyl-CoA and oxaloacetate.

MSC: Applying
23. Predict the fate of acetyl-CoA and oxaloacetate when the citrate cycle is inhibited.
ANS:
Acetyl Co-A is used in the cytosol for cholesterol and fatty acid biosynthesis. Oxaloacetate
can either be converted to malate in the cytosol by malate dehydrogenase or it can be
converted to phosphoenolpyruvate by phosphoenolpyruvate carboxykinase for
gluconeogenesis. Oxaloacetate also functions as a precursor to the amino acids aspartate and
glutamate.

24. Compare and contrast the anaplerotic nature of the pyruvate carboxylase reaction and the
phosphoenolpyruvate carboxylase reaction.
ANS:
Both reactions help replenish oxaloacetate in the citrate cycle. The pyruvate carboxylase
reaction replenishes oxaloacetate from pyruvate. Phosphoenolpyruvate carboxylase
replenishes the citrate cycle intermediate from the reactants phosphoenolpyruvate and
bicarbonate.

MSC: Analyzing
33
25. In the following figure, identify and explain the specific pathways (A–F) that are shared with
the citrate cycle intermediates.
ANS:
A. Succinyl-CoA and glycine synthesize -aminolevulinic acid via -aminolevulinic acid
synthase, which is an essential component for heme biosynthesis.
B. -Ketoglutarate undergoes a transamination reaction to form the carbon backbone of the
amino acids aspartate and glutamate.
C. Oxaloacetate undergoes a transamination reaction to form the carbon backbone of the
amino acids aspartate and glutamate.
D. Oxaloacetate is a substrate for phosphoenolpyruvate carboxykinase, generating
phosphoenolpyruvate for glucose synthesis.
E. Acetyl Co-A is used in fatty acid biosynthesis.*
F. Acetyl Co-A is used in cholesterol biosynthesis.*
*Note: E and F can be interchangeable.

and succinyl-CoA in the cell. MSC: Understanding
34

Biochemistry 1st Edition Miesfeld Test Bank

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Biochemistry 1st Edition Miesfeld Test

1. Which molecules function as electron acceptors in the citrate cycle?

3. The primary function of NAD+ in the citrate cycle is that it

5. Where do citrate cycle reactions in eukaryotic cells take place?

15. Which enzyme in the citrate cycle produces NADH?

16. Which enzyme requires CoASH to produce acetyl-CoA?

21. In linked metabolic pathways, the oxidants in subsequent reactions must

22. Coenzyme A is derived from which of the following vitamins?

26. The disease beriberi is a result of which vitamin deficiency?

41. How is the pyruvate dehydrogenase reaction regulated?

60. In the citrate cycle, a high concentration of NADH would result in

65. The citrate cycle is considered to be a(n) __________ pathway.

74. Which citrate cycle intermediate is also used in gluconeogenesis?

DIF: Medium REF: 10.1

DIF: Medium REF: 10.1

DIF: Difficult REF: 10.1

DIF: Difficult REF: 10.1

DIF: Medium REF: 10.1

Then, use this value to determine Gibbs free energy.

G° = –(2)(96.48 kJ/V mol)(+0.15 V)

DIF: Difficult REF: 10.1

DIF: Medium REF: 10.1

DIF: Difficult REF: 10.2

DIF: Medium REF: 10.2

10. Explain why riboflavin is critical to the citrate cycle.

DIF: Medium REF: 10.2

DIF: Difficult REF: 10.2

DIF: Difficult REF: 10.2

13. Explain how arsenic affects the pyruvate dehydrogenase reaction.

DIF: Medium REF: 10.2

DIF: Difficult REF: 10.2

DIF: Difficult REF: 10.2

DIF: Difficult REF: 10.2

DIF: Medium REF: 10.3

DIF: Difficult REF: 10.3

DIF: Medium REF: 10.4

DIF: Medium REF: 10.4

DIF: Easy REF: 10.4

DIF: Medium REF: 10.5

DIF: Medium REF: 10.5

DIF: Difficult REF: 10.5

DIF: Difficult REF: 10.5

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