Chapter 10: Hemoglobin: Protein Function in Microcosm

Matching
A)

positively cooperative

B)

cyanosis

C)

His E7

D)

decrease

E)

F)

hydrogen bonds

G)

increase

H)

symmetry

I)

His F8

J)

ion pairs

K)

L)

hemolytic anemia

1. In the ______ form of hemoglobin, the iron ion is out of the plane of the porphyrin ring.
Ans: K
Level of Difficulty: Easy
Section 10-2. Structure and Mechanism
2. The conversion of hemoglobin from the T to the R form involves breaking C-terminal ______.
Ans: J
Level of Difficulty: Easy
Section 10-2. Structure and Mechanism
3. An increase in pCO2 causes hemoglobin's affinity for oxygen to ______.
Ans: D
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
4. Hemoglobin's subunits bind oxygen in a ______ manner.
Ans: A
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function

5. The absence of 2,3-BPG causes hemoglobin's affinity for oxygen to______.

Ans: G
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
6. The ______ model of allosterism requires subunits to change conformation simultaneously.
Ans: H
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
7. Sickle cell hemoglobin does not form fibers in the ______ form.
Ans: E
Level of Difficulty: Easy
Section 10-1. Hemoglobin and Myoglobin Function
8. When unstable hemoglobins are degraded, the products often cause cell lysis, leading to a condition
called ______.
Ans: L
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
9. When oxygen binds to heme, the oxygen forms a hydrogen bond with ______.
Ans: C
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
10. Mutations that favor the oxidation of the heme iron to the +3 oxidation state can cause ______.
Ans: B
Level of Difficulty: Moderate
Section: 10-3. Abnormal Hemoglobins

Multiple Choice
11. Which of the following is not a ligand to the porphyrin ring Fe2+ ion in oxymyoglobin?
A) His E7
B) His F8
C) Nitrogen atoms in the porphyrin ring
D) Oxygen
E) all are ligands
Ans: A
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
12. Which gas does not bind to the porphyrin ring Fe2+ ion in myoglobin?
A) NO
B) CO
C) CO2
D) O2

E) H2S
Ans: C
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
13. Which of the following statements does not apply to the K value in the equation for the oxygen
binding curve of myoglobin?
A) It is numerically equal to p50.
B) It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied.
C) It is a measure of the affinity of myoglobin for oxygen.
D) If Y > K, then myoglobin is less than 50% saturated with oxygen.
E) It is the value of pO2 at which Y = 0.5.
Ans: D
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
14. When the partial pressure of oxygen in venous blood is 30 torr, the YO2 value for myoglobin is ______
while the YO2 value for hemoglobin is ______.
A) 0.55, 0.91
B) 0.91, 0.55
C) 2.8 torr, 26 torr
D) 0.91, 0.97
E) none of the above
Ans: B
Level of Difficulty: Moderate
Section: 10-1. Hemoglobin and Myoglobin Function
15. Myoglobin and a single chain of hemoglobin have similar ______ structures.
A) primary
B) secondary
C) tertiary
D) quaternary
E) none of the above
Ans: C
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
16. Hemoglobin's p50 value is about ______ as great as myoglobin's p50 value.
A) one-tenth
B) half
C) twice
D) ten times
E) twenty times
Ans: D
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function

17. The value of n in the Hill equation for hemoglobin is about ______ as great as the value for
myoglobin.
A) half
B) twice
C) three times
D) five times
E) ten times
Ans: C
Level of Difficulty: Moderate
Section: 10-1. Hemoglobin and Myoglobin Function
18. Consider a hypothetical hemoglobin with a Hill coefficient of 1 and the same p50 value as normal
hemoglobin. Choose the statement below that best describes the two proteins.
A) There is a cooperative interaction between oxygen-binding sites in both the hypothetical and normal
hemoglobins.
B) The hypothetical hemoglobin has a greater oxygen affinity than normal hemoglobin.
C) The oxygen binding curve for the hypothetical hemoglobin is hyperbolic, and the curve for normal
hemoglobin is sigmoidal.
D) The two hemoglobins would be able to deliver about the same amount of oxygen to the tissues.
E) At pO2 less than p50, normal hemoglobin has a greater YO2 value.
Ans: C
Level of Difficulty: Moderate
Section: 10-1. Hemoglobin and Myoglobin Function
19. Some abnormal hemoglobins have Hill coefficients that are ______ that of normal hemoglobin,
indicating that their ability to bind oxygen cooperatively has been compromised.
A) less than
B) greater than
C) much greater than
D) about equal to
E) cannot be determined from the information given
Ans: A
Level of Difficulty: Moderate
Section: 10-1. Hemoglobin and Myoglobin Function
20. The Hill plot shows that the fourth oxygen binds to hemoglobin with ______-fold greater affinity
than the first.
A) 2
B) 5
C) 10
D) 20
E) 100

Ans: E
Level of Difficulty: Moderate
Section: 10-1. Hemoglobin and Myoglobin Function
21. Myoglobins secondary structure is primarily composed of ______________.
A) parallel -sheets
B) antiparallel -sheets
C) -helices
D) -bends
E) -helices
Ans: C
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
22. Myoglobins primary physiological role is to facilitate oxygen ________.
A) storage
B) metabolism
C) binding
D) reduction
E) diffusion
Ans: E
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
23. If the gene for myoglobin is knocked out in mice, the mice:
A) have larger lungs.
B) respire extremely rapidly.
C) have dark brown muscle tissue.
D) appear normal, with lighter colored muscle tissue.
E) have their growth stunted.
Ans: D
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
24. Carbon monoxide binds to Heme:
A) with a higher affinity than oxygen.
B) resulting in the oxidation of the Fe(II) to Fe(III)
C) in a manner that displaces carbon dioxide, causing CO 2 poisoning.
D) from the side opposite oxygen, resulting in a brown colored heme.
E) with a lower affinity than oxygen.
Ans: A
Level of Difficulty: Easy

Section: 10-1. Hemoglobin and Myoglobin Function

25. The primary structure of mammalian hemoglobin, an 22 tetramer, is approximately _____
identical to myoglobin.
A) 2%
B) 18%
C) 50%
D) 78%
E) 98%
Ans: B
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
26. In sickle-cell anemia, the negatively charged glutamic acid residue is replaced by the neutral amino
acid ____________.
A) tyrosine
B) lysine
C) valine
D) adenosine
E) glycine
Ans: C
Level of Difficulty: Easy
Section: 10-3. Abnormal Hemoglobins
27. Which of the following increases the affinity of hemoglobin for oxygen:
A) an increase in BPG concentration.
B) the formation of N-terminal carbamates.
C) increasing pH.
D) all of the above
E) none of the above
Ans: C
Level of Difficulty: Moderate
Section: 10-2. Structure and Mechanism
28. The most rapid way that erythrocytes adapt to high altitudes is:
A) by producing genetically altered hemoglobins that have higher O2-binding affinities.
B) by adopting the symmetry model of allosterism.
C) by increasing the concentration of hemoglobin.
D) by relying upon the simpler protein myoglobin.
E) by increasing the intracellular concentration of BPG.
Ans: E
Level of Difficulty: Easy

Section: 10-1. Hemoglobin and Myoglobin Function

29. Hemerythrin and hemocyanin are:
A) human mutant hemoglobins with decreased oxygen affinity.
B) hemoglobin variants that are found in animals at high altitude.
C) synthetic derivatives of hemoglobins heme group used in artificial blood substitutes.
D) oxygen transport proteins found in invertebrates.
E) tetrameric hemoglobin derivatives containing only -chains ( 4 tetramers).
Ans: D
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
30. The rearrangement of T-form hemoglobin to the R-form:
A) occurs in each protein subunit independently when its heme binds oxygen.
B) requires the binding of at least three oxygen molecules.
C) increases the ion pairing interactions of the C-terminal amino acids.
D) involves the movement of the Fe(II) into the heme plane.
E) opens a central cavity for BPG binding.
Ans: D
Level of Difficulty: Moderate
Section: 10-2. Structure and Mechanism
31. Max Perutz investigation of the structure and function of hemoglobin primarily utilized___.
A) X-ray crystallography
B) NMR spectroscopy
C) genomics
D) mass spectroscopy
E) genetic engineering
Ans: A
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
32. While the binding of O2 to myoglobin as a function of pO2 is described by a simple __________
curve, the binding to hemoglobin is described by a more complex ______ curve.
A) sigmoidal; hyperbolic
B) hyperbolic; sigmoidal
C) exponential; hyperbolic
D) sigmoidal; bell-shaped
E) hyperbolic; concave
Ans: B
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism

33. Hemoglobin S, the variant responsible for the misshapen red blood cells characteristic of the disease
sickle-cell anemia, is potentially advantageous to heterozygotes because it confers some level of
resistance to the disease _________.
A) rickets
B) AIDS
C) cyanosis
D) polycythemia
E) malaria
Ans: E
Level of Difficulty: Easy
Section: 10-3. Abnormal Hemoglobins
34. Which of the following is not true for the symmetry model of allosterism:
A) the protein is an oligomer of symmetrically (or pseudosymmetrically) related subunits.
B) the oligomer can exist in two conformational states which are in equilibrium.
C) the ligand can bind to a subunit in either conformation.
D) the molecular symmetry of the protein is conserved during the conformational change.
E) none of the above.
Ans: E
Level of Difficulty: Easy
Section: 10-4. Allosteric Regulation
35. BPG stands for:
A) biphenylglycine
B) boronylphenylglutamate
C) bisphosphoglycerate
D) bisphenylglycerol
E) betapropylglutamine
Ans: C
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
36. Why is the decreased affinity of fetal hemoglobin for BPG advantageous?
A) With fewer BPG molecules bound there are more heme residues available for O 2 binding.
B) Decreased BPG binding biases the fetal hemoglobin toward the R state.
C) More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state.
D) BPG is available to bind to fetal myoglobin, helping to release O 2 in fetal muscle tissue.
E) none of the above
Ans: B
Level of Difficulty: Moderate
Section: 10-1. Hemoglobin and Myoglobin Function

37. During the T to R conformational shift, Fe(II) drags the F-helix via a bond to the side chain of
________.
A) Leu F7
B) Leu F4
C) His F8
D) Leu FG3
E) Val FG5
Ans: C
Level of Difficulty: Easy
Section: 10-2. Structure and Mechanism
38. If the binding of O2 to hemoglobin was characterized by a Hill constant of -1:
A) hemoglobin would not be able to release bound O2.
B) the O2 binding curve would be hyperbolic.
C) the sequential model of allosterism would be eliminated as a reasonable model.
D) the binding of the first O2 would decrease the affinity of the hemoglobin for O 2.
E) the binding of the first O2 would increase the affinity of the hemoglobin for O2.
Ans: D
Level of Difficulty: Easy
Section: 10-1. Hemoglobin and Myoglobin Function
39. ______of the worlds human population carry a variant hemoglobin.
A) 5%
B) 25%
C) 50%
D) 75%
E) 90%
Ans: A
Level of Difficulty: Easy
Section: 10-3. Abnormal Hemoglobins