MCQS ON HEMOGLOBIN AND

MYOGLOBIN
When oxygen binds to a heme-containing protein, the two open
coordination bonds of Fe2+ are occupied by:

A) one O atom and one amino acid atom.

B) one O2 molecule and one amino acid atom.

C) one O2 molecule and one heme atom.

D) two O atoms.

E) two O2 molecules.

ANSWER = B

In the binding of oxygen to myoglobin, the relationship between the

concentration of oxygen and the fraction of binding sites occupied can
best be described as:

A) hyperbolic.

B) linear with a negative slope.

C) linear with a positive slope.

D) random.

E) sigmoidal

ANSWER = A

Myoglobin and the subunits of hemoglobin have

A) no obvious structural relationship

B) very different primary and tertiary structures

C) very similar primary and tertiary structures.

D) very similar primary structures, but different tertiary structures

E) very similar tertiary structures, but different primary structures

ANSWER = E
In hemoglobin, the transition from T state to R state (low to high affinity)
is triggered by

A) Fe" binding.

B) heme binding

C) oxygen binding

D) subunit dissociation

E) subunit association

ANSWER = C

Which of the following is not correct concerning 2.3-

bisphosphoglycerate (BPG)

A) It binds at a distance from the heme groups of hemoglobin

B) It binds with lower affinity to fetal hemoglobin than to adult

hemoglobin.

C) It increases the affinity of hemoglobin for oxygen

D) It is an allosteric modulator.

E) It is a normally found associated with the hemoglobin extracted from

red blood cells.

ANSWER = C

After releasing O2 at the tissues, hemoglobin transports

A) CO2 and protons to the lungs

B) O2 to the lungs

C) CO2 and protons to the tissue

D) Nutrients

ANSWER = A

A Haemoglobin contains about

A 30% of the total body iron

B) 50% of the total body iron

C) 75% of the total body iron

D) 90% of the total body iron

ANSWER = C

About 5% of the total body, iron is present in

A) Transferrin

B) Myoglobin

C) Cytochromes

D) Hemosiderin

ANSWER = B

Each haemoglobin molecule contains

A) One iron atom

B) Two iron atoms

C) Four iron atoms

D) Six iron atoms

ANSWER = C

EACH myoglobin molecule contains

A) One iron atom

B) Two iron atoms

C) Four iron atoms

D) Six iron atoms

ANSWER = A

Carbon monoxide (CO) is toxic to humans because:

A) it binds to myoglobin and causes it to denature

B) it is rapidly converted to toxic CO2

C) it binds to the globin portion of hemoglobin and prevents the binding

of O2

D) it binds to the Fe in hemoglobin and prevents the binding of O2

E) it binds to the heme portion of hemoglobin and causes heme to unbind
from hemoglobin

ANSWER = D

Cyanmethaemoglobin can be formed from

A) Oxy Hb

B) Met Hb

C) Carboxy Hb

D) All of these

ANSWER = B

In thalassemia, an amino acid is substituted in

A) Alpha chain

B) Beta chain

C) Alpha and beta chains

D) Any chain

ANSWER = D

The amino acid substitution of Val for Glu in Hemoglobin S results in

aggregation of the protein because of ___________ interactions between
molecules .

A) covalent

B) disulphide

c) hydrogen bonding

D) hydrophobic

E) Ionic

ANSWER = D

The fundamental cause of sickle-cell disease is a change in the structure

of

A) blood

B) capillaries
C) hemoglobin

D) red cells.

E) the heart

ANSWER = C

In the binding of oxygen to myoglobin, the relationship between the

concentration of oxygen and the fraction of binding sites occupied can
best be described as:

A) hyperbolic

B) linear with a negative slope

C) linear with a positive slope

D) random

E) sigmoidal

ANSWER = A

Carboxyhemoglobin is formed by

A) CO

B) CO2

C) HCO3

D) HCN

ANSWER = A

Methemoglobin is formed as a result of the oxidation of haemoglobin by

oxidation agent:

A) Oxygen of Air

B) H2O2

C) K4Fe(CN)6

D) KMnO4

ANSWER = C

Methemoglobin can be reduced to haemoglobin by

A) Removal of hydrogen

B) Vitamin C

C) Glutathione

D) Creatinine

ANSWER = B

Protein present in hemoglobin has the structure known as

A) Primary

B) Secondary

C) Tertiary

D) Quaternary

ANSWER = D

Foetal haemoglobin contains

A) Two α and two γ chains

B) Two β and two γ chains

C) Both (A) and (B)

D) None of these

ANSWER = A

Abnormal chain of amino acids in sickle cell anaemia is

A) Alpha chain

B) Beta chain

C) Delta chain

D) Gama chain

ANSWER = B

Number of chains in globin part of normal Hb:

A) 1

B) 2
C) 3

D) 4

ANSWER = D

When haemoglobin takes up oxygen there is a change in the structure

due to the moving closer together of

A) β-chains

B) α-chains

C) γ-chains

D) α and γ chains

ANSWER = A

Myoglobin and the subunits of hemoglobin have:

a) Very different primary and tertiary structures

b) Very similar primary and tertiary structures

c) Very similar primary structures, but different tertiary structures

d) Very similar tertiary structures, but different primary structures

ANSWER = D (Hemoglobin is a tetramer and myoglobin is a monomer.)

Myoglobin binding of oxygen depends on:

A) the oxygen concentration (pO2)

B) the hemoglobin concentration

C) the affinity of myoglobin for the O2 (K)

D) a) and c)

E) a), b) and c)

ANSWER = D

Type of thalassemia that is caused by decrease or total absence of alpha

globulin chains of HB is termed as

A) Thalassemia

B) Alpha thalassemia
C) Beta thalassemia

D) Sickle cell anaemia

ANSWER = B

What contains 2 alpha chains and 2 beta chains that assume a

quaternary higher order conformation?

A) Maternal hemoglobin

B) Myoglobin

C) Immunoglobin

D) Fetal hemoglobin

ANSWER = A

Which of the following is in red muscle and consists of a single

polypeptide with a prosthetic heme group?

A) Maternal hemoglobin

B) Myoglobin

C) Immunoglobin

D) Fetal hemoglobin

ANSWER = B

If iron in hemoglobin is oxidized to 3+, what disease may occur?

A) Sickle cell anemia

B) Methemoglobinemia

C) Carbon monoxide poisoning

D) Cystic fibrosis

ANSWER = B

When binding with oxygen, what type of binding curve does myoglobin
have?

A) Linear

B) Sigmoidal
C) Hyperbolic

D) It has none

ANSWER = C

When binding with oxygen, what type of binding curve does hemoglobin
have?

A) Linear

B) Sigmoidal

C) Hyperbolic

D) It has none

ANSWER = B

When will hemoglobin have the highest affinity for oxygen?

A) When pH is low

B) When carbon monoxide levels are high

C) At high elevations

D) When 2,3-bisphosphoglycerate levels are low

ANSWER = D

What phenomenon occurs when decreased ph causes hemoglobin to

release oxygen into tissues?

A) Allosteric effect

B) ELISA

C) Bohr shift

D) Western blotting

E) Both B and D

ANSWER = B

What consists of 2 alpha chains and 2 gamma chains?

A) Maternal hemoglobin

B) Myoglobin
C) Immunoglobin

D) Fetal hemoglobin

ANSWER = D

What has the highest affinity for oxygen?

A) Maternal hemoglobin without 2,3-bisphosphoglycerate

B) Myoglobin

C) Maternal hemoglobin with 2,3-bisphosphoglycerate

D) Fetal hemoglobin with 2,3- bisphosphoglycerate

ANSWER = B

A point mutation in the beta-globin gene changing the codon from

glutamate to valine will likely cause what disease?

A) Sickle cell anemia

B) Methemoglobinemia

C) Carbon monoxide posioning

D) Cystic fibrosis

ANSWER = A

Which of the following is false?

A) The binding curve of oxygen and hemoglobin is sigmoidal for a patient

with carbon monoxide poisoning

B) In the presence of 2,3-bisphosphoglycerate, the affinity for oxygen in

fetal hemoglobin is unaffected

C) Myoglobin does not use an allosteric effect

D) The allosteric effect will increase the binding of oxygen to hemoglobin

E) None of the above

ANSWER = E
Which of the following is true?

A) Hemoglobin is involved in transporting oxygen

B) Myoglobin is involved in oxygen storage

C) Compared to oxygen, carbon monoxide has a higher affinity for

hemoglobin

D) A, B and C

E) A and C

ANSWER = D

A Hemoglobin (Hb) molecule is a tetramer consisting of four polypeptide

chains, 2 alpha and 2 Beta chains. Each Hb subunit contains a single
heme moiety consisting of a protoporphyrin complexed with a single
iron in order to bind oxygen.. Each heme can bind how many oxygen
molecules and transport a total of ____ oxygen molecules.

A) One: Two

B) One: Four

C) Two: Four

D) Two: eight

ANSWER = B

Hemoglobin Fetal (2 alpha, 2 gamma HgF)) synthesis predominantly

occurs during the fetal life and constitute 70% of total Hb at
birth. Produced by foetus in utereo until about 48 weeks after
birth. Has a high oxygen affinity oxygen delivering oxygen to the
foetus. After birth, __________ production rapidly increases and HbF
production drops off.

A) Hemoglobin S

B) Hemoglobin A

C) Hemoglobin G

D) Hemoglobin B

ANSWER = B (Hemoglobin A (HbA) : Adult, by 3months of age almost all

the Hb is adult type)
Variant is an Hb that contains a change. These can be benign or cause
disease. Most variants result in a single aa substitution resulting from a
point mutation.

A) True

B) False

ANSWER = A

Sickle Cell Disease is an Autosomal recessive disorder. The pathogenesis

of the Glu to Val substitution. Decreases solubility of deoxygenated Hb.
This causes a stiff fibrous polymers that distort RBCs giving a sickle cell
shape. Sickle cell occludes the capillaries and cause __________ and
__________.

A) Ischemia and infractions

B) Platelets build up and clotting factors

C) Factor V and Plasminogen

ANSWER = A

Irreversible sickled cells that are not removed by the spleen are removed
by the liver.

A) True

B) False

ANSWER = B (Repeated sickling and unsickling produce irreversible

sickled cells that are removed by the spleen. The rate of removal exceeds
the production leading to anaemia)

Sickle cell can be detected in blood smears. Definitive diagnosis are

made by __________

A) Hb electrophoresis showing low level of HbS < 80%

B) Hb electrophoresis showing high level of HbS > 80%

ANSWER = B
Compound heterozygote is 1 parent having HbS allele and other HbC
allelle =

A) Sickle hemoglobin C disease (HbSC)

B) Sickle B+ Thalassemia

C) Sickle B* Thalassemia

D) Sickle Hemoglobin SS disease

ANSWER = A ( Sickle HbSC is usually milder in severity of the disease

compared to HbSS. Sickle Beta Thalassemia: the sickle cell allele
inherited from one parent and the B allele from other parent. Sickle Beta
Thalassemia: No production of Beta)

Beta Thalassemia has no beta globin expression.

A) True

B) False

ANSWER = A

Hemoglobin S (HbS) is on the Beta chain: residue 6 substituting a

A) Glu to Lys

B) Glu to Val

C) Val to Glu

D) Lys to Glu

ANSWER = B

Hemoglobinopathies have two categories: Disorder of Hb structure and

Hb synthesis.

A) True

B) False

ANSWER = A
Which one of the following statements concerning the hemoglobin is
correct?

A) HbA is the most abundant hemoglobin in normal adults.

B) Fetal blood has a lower affinity for oxygen than does adult blood
because HbF has an increased affinity for 2,3-bisphosphoglycerate.

C) The globin chain composition of HbF is α2δ2.

D) HbA1c differs from HbA by a single, genetically determined amino acid

substitution.

E) HbA2 appears early in fetal life.

ANSWER = A

Which one of the following statements concerning the ability of acidosis

to precipitate a crisis in sickle cell anemia is correct?

A) Acidosis decreases the solubility of HbS.

B) Acidosis increases the oxygen affinity of hemoglobin.

C) Acidosis favors the conversion of hemoglobin from the taut to the

relaxed conformation.

D) Acidosis shifts the oxygen-dissociation curve to the left.

E) Acidosis decreases the ability of 2,3 -bisphosphoglycerate to bind to

hemoglobin

ANSWER = A

Which one of the following statements concerning the binding of

oxygen by hemoglobin is correct?

A) The Bohr effect results in a lower oxygen affinity at higher pH values.

B) Carbon dioxide increases the oxygen affinity of hemoglobin by

binding to the C-terminal groups of the polypeptide chains.

C) The oxygen affinity of hemoglobin increases as the percentage

saturation increases.

D) The hemoglobin tetramer binds four molecules of 2,3-

bisphosphoglycerate.
E) Oxyhemoglobin and deoxyhemoglobin have the same affinity for
protons.

ANSWER = C

β-Lysine 82 in HbA is important for the binding of 2,3-

bisphosphoglycerate. In Hb Helsinki, this amino acid has been replaced
by methionine. Which of the following should be true concerning Hb
Helsinki?

A) It should be stabilized in the taut, rather than the relaxed, form.

B) It should have increased oxygen affinity and, consequently, decreased

oxygen delivery to tissues.

C) Its oxygen-dissociation curve should be shifted to the right relative to

HbA.

D) It results in anaemia.

ANSWER = B

A 67-year-old man presented to the emergency department with a 1-

week history of angina and shortness of breath. He complained that his
face and extremities had taken on a blue color. His medical history
included chronic stable angina treated with isosorbide dinitrate and
nitroglycerin. Blood obtained for analysis was brown. Which one of the
following is the most likely diagnosis?

A) Carboxyhemoglobinemia

B) Hemoglobin SC disease

C) Methemoglobinemia

D) Sickle cell anemia

E) β-Thalassemia

ANSWER = C .

A 27-year-old firefighter is brought to the emergency room after being

exposed to smoke during a training exercise. He looks ill and has labored
breathing. He is clutching his head and exhibits an altered mental status.
On examination, you note that he appears red, and his pulse oximetry
reads 100%. You suspect carbon monoxide toxicity. What is true of the
oxygen saturation curve during carbon monoxide toxicity?
A) The oxygen saturation curve is shifted to the left.

(B) The oxygen saturation curve is shifted to the right.

C) The effect of carbon monoxide on hemoglobin is similar to that of

having increased levels of 2,3- bisphosphoglycerate.

D) The effect of carbon monoxide on hemoglobin is similar to that of a

low pH state.

E) The effect of carbon monoxide on hemoglobin is similar to that of an

increased temperature state.

ANSWER = A

In deoxyhemoglobin (Hb), the Fe (II) is 5-coordinated to:

A) four nitrogen of heme and to the proximal His. of Hb

B) four nitrogen of heme and to a water molecule

C) four nitrogen of heme and to an O2 molecule

D) two nitrogen of heme and to three His. residues in Hb

E) two nitrogen of heme and to three water molecules

ANSWER = A

Spontaneous oxidation of the heme-bound Fe(II) to Fe(III) is prevented in

hemoglobin by :

A) the symmetry of its quaternary structure

B) the four heme-protein covalent bonds.

C) a highly-ordered water molecule within the heme pocket

D) the surrounding protein structure in each subunit

E) methemoglobin reductase

ANSWER = D

In sickle cell anemia, the basis of the malfunction of the hemoglobin

molecule is :

A) incorrect secondary structure

B) substitution of a single amino acid

C) faulty binding of the heme groups

D) reduced affinity for oxygen

E) insufficient iron in the diet.

ANSWER = B

Allosteric effects that occur in hemoglobin:

A) only occur in humans

B) are important for maintaining Fe in the Fe2+ state

C) minimize oxygen delivery to the tissues.

D) optimize oxygen delivery to the tissues

E) can also be observed in myoglobin

ANSWER = D

The following small molecules affect hemoglobin as indicated:

A) Decreased [H+] and [N3-] decrease Hb affinity for O2

B) Increased [H+] and [C1-] increase Hb affinity for O2

C) Increased [C0] and [C1-] increase Hb affinity for O2

D) Increased [H+] and [C1-] decrease Hb affinity for O2

E) Decreased [bisphosphoglycerate] (BPG) decreases the affinity for O2

ANSWER = D

The cooperativity of O2 binding to hemoglobin results in a :

A) 100-fold higher affinity for the last O2 bound than for the first

B) 100-fold lower affinity for the last O2 bound than for the first

C) extensive protein conformational change

D) release of H+ with the dissociation of O2

E) the first and third choices are both correct.

ANSWER = E
Hemoglobin has a high content of this amino acid:

A) Proline

B) Leucine

C) Arginine

D) Histidine

ANSWER = D

The lone pair of electrons at one of the ring nitrogens in the given amino
acid makes a potential ligand, which is important in binding the iron
atoms in hemoglobin:

A) Tryptophan

B) Threonine

C) Histidine

D) Serine

ANSWER = C

Which hemoglobin is increased with THALASSEMIA?

A) Hgb A

B) Hgb F

C) Hgb S

D) Hgb SC

E) Hgb C

ANSWER = B

Sickle cell - Equatorial Africa, malaria protection

A) Hgb A

B) Hgb F

C) Hgb S

D) Hgb SC

E) Hgb C
ANSWER = C

Sickle Cell Disease

A) Homozygotes

B) Heterozygotes

ANSWER = A

Sickle Cell Trait

A) Homozygotes

B) Heterozygotes

ANSWER = B

All Hgb is structurally abnormal (due to incorrect amino acid in beta

globin chain): called Hgb S

A) Homozygotes

B) Heterozygotes

ANSWER = A

Which of the following is NOT true of sickle cell anemia?

A) Can present with intense ischemic pain in chest, back, abdomen, and
bones due to occlusion of small vessels by sticky, sickled RBCs in
different tissues; fever; nausea and vomiting

B) Precipitated by deoxygenation; infection; dehydration; often no

identifiable reason

C) Can result in multiorgan tissue death and complications in many

organs

D) Presents with a normal Hgb S band with hemoglobin electrophoresis

E) All of these things are true of sickle cell anemia

ANSWER = D
Presents with intense ischemic pain in chest, back, abdomen, and bones
due to occlusion of small vessels; fever; nausea and vomiting

A) Sickle Cell Anemia

B) Vitamin B12 Deficiency Anemia

C) Folate Deficiency Anemia

D) Sequestration

ANSWER = A

A family of four from New Jersey has embarked on a vacation in the

Rocky Mountains. All four required a 24 to 48 hour acclimation to the
high altitude, as all were breathing at a rapid pace until the acclimation
took effect. In addition to increasing the number of red blood cells in
circulation, what other compensatory mechanism occurred within the
red blood cell during this acclimation period?

A) Increased synthesis of lactic acid

B) Decreased synthesis of lactic acid

C) Increased synthesis of 2,3-bisphosphoglycerate

D) Decreased synthesis of 2,3-bisphosphoglycerate

E) Decreased degradation of bilirubin, producing less carbon monoxide

ANSWER = C : Increased synthesis of 2,3-bisphosphoglycerate.

2,3-bisphosphoglycerate (2,3-BPG) will bind to and stabilize the

deoxygenated form of hemoglobin. Thus, if 2,3-BPG levels are increased,
the binding of this molecule will aid in removing oxygen from
hemoglobin in the tissues (where the concentration of oxygen is low)
and therefore increase oxygen delivery to the tissues. In the lungs,
where the oxygen concentration is high, the high levels of oxygen can
overcome the effects of 2,3-BPG and bind to hemoglobin. Lactic acid
levels do not directly affect oxygen binding (and lactate does not
accumulate in the red cell), although changes in proton concentration
(pH) can. Decreased pH will reduce oxygen binding to hemoglobin due to
the Bohr effect. Bilirubin degradation, even though it does produce CO,
does not effect oxygen binding to hemoglobin.
You see a patient on an initial visit and are struck by the bluish coloring
of the skin and mucous membranes. You ask the patient about this and
you are told that it is a blood problem that the patient has had for his or
her entire life. The patient’s father had a similar condition, but not the
mother. This condition could result from which one of the following
changes within the erythrocyte?

(A) An increase of 2,3-bisphosphoglycerate in the erythrocyte

(B) An E to V mutation at position 6 of the β-chain of hemoglobin

(C) Increased oxidation of heme iron to the +3 state

(D) Enhanced oxygen binding to hemoglobin

(E) A mutated hemoglobin which no longer exhibited the Bohr effect

ANSWER = C : Increased oxidation of heme iron to the +3 state.

The patient is exhibiting methemoglobinemia, in which an increased

percentage of his hemoglobin has the iron in the +3 oxidation state
(normal is +2), which is a form that cannot bind oxygen. This condition
can arise by a variety of mutations within hemglobin which lead to
destabilization of the iron in the heme ring. The red blood cell contains
methemoglobin reductase, which will reduce the iron back to the +2
state (using NADPH as the electron donor), and mutations within the
reductase can also lead to this condition. An acquired form of
methemoglobinemia can be caused by exposure to oxidizing drugs or
toxins (aniline dyes, nitrates, nitrites, and lidocaine) which exceed the
reduction capacity of the red blood cells. Surprisingly, the majority of
patients with this syndrome show no ill effects, other than the bluish
discoloration of certain tissues. Excessive 2,3-bisphosphoglycerate in
the erythrocyte would lead to increased oxygen delivery to the tissues
as 2,3-bisphosphoglycerate stabilizes the deoxygenated form of
hemoglobin (as would a mutant hemoglobin with an enhanced ability to
bind 2,3-BPG). The E to V mutation at position 6 of the β-chain of
hemoglobin leads to sickle cell disease
A 7-year-old African American male is admitted to the hospital with
severe abdominal pain. A blood workup indicated anemia, and an
abnormal blood smear (see below). The molecular event triggering this
disease is which of the following?

A) A loss of quaternary structure of the hemoglobin molecule

B) An increase in oxygen binding to hemoglobin

C) A gain of ionic interactions, stabilizing the “T” form of hemoglobin

D) An increase in hydrophobic interactions between deoxyhemoglobin

molecules

E) An alteration in hemoglobin secondary structure leading to loss of the

“α” helix

ANSWER = D : An increase in hydrophobic interactions between

deoxyhemoglobin molecules.
The boy is suffering from sickle cell anemia, which is due to a
substitution of valine for glutamate at position 6 of the β-chain. This
change, from a negatively charged amino acid side chain (glutamate) to a
hydrophobic side chain (valine), allows deoxygenated hemoglobin to
polymerize and form long rods within the red blood cell. Deoxygenated
hemoglobin has a hydrophobic patch on its surface (created by A70, F85,
and L88), which the valine in position 6 on another hemoglobin chain can
associate with via hydrophobic interactions (this does not occur in
normal hemoglobin as there is a charged glutamate residue at this
position, which will not interact with a surface hydrophobic patch––see

the figure below). The binding of hemoglobin molecules to each other

results in the polymerization. Oxygenated hemoglobin does not present
a hydrophobic surface to other hemoglobin molecules, so
polymerization is much less likely in the oxygenated state. The
polymerization is not caused by a loss of quaternary structure, an
increase in oxygen binding (which would actually reduce sickling), a gain
of ionic interactions, or the loss of any α-helical structure in the final
conformation of the protein.
In Hb S, glutamic acid replaced by valine. What will be its electrophoretic
mobility?

A) Increased

B) Decreased

C) No change

D) Depends on level of concentration of Hb S

ANSWER = B : Decreased

In Hb S, Glutamic acid is replaced by Valine. Hence the negative charge is

decreased. So Hb S moves slower than HbA1.The relative mobility of
various Hb fractions in Hb electrophoresis. Relative mobility of common
hemoglobin fractions from origin or point of application is

1. Hb A2, 2. Hb S, 3.Hb F, 4. HbA1

All of the following are true about sickle cell disease, except :

A) Single nucleotide change results in change of Glutamine to Valine

B) RFLP result from a single base change

C) ‘Sticky patch’ is generated as a result of

replacement of a nonpolar residue with a polar residue

D) Hb S confers resistance against malaria in heterozygotes.

ANSWER = C

‘Sticky patch’ is generated as a result of replacement of a nonpolar

residue with a polar residue Sickle Cell Anemia (Hb S)