Myoglobin and hemoglobin each have different numbers of subunits and this affects their respective
oxygen storage and delivery capabilities. How many subunits do myoglobin and hemoglobin each have?
Select one:
a. Two, Three
b. One, Two
c. One, Four Correct! Myoglobin consist of one and hemoglobin consists of four subunits. The
number of subunits affects their respective oxygen storage and delivery capabilities.
d. Four, One
Addition of alters the shape of the iron–heme complex, and therefore its
absorption of light as indicated by its color change from dark purple (the color of hemoglobin in
venous blood) to brilliant scarlet (the color of hemoglobin in arterial blood).
Select one:
a. iron
b. oxygen Correct!
c. globin subunit
d. porphyrin
Oxygen binding alters the structure of an entire hemoglobin tetramer, so the structures of oxyhemoglobin
and deoxyhemoglobin are noticeably different. The oxyhemoglobin conformation is specifically referred
to as the state, whereas the deoxyhemoglobin conformation is referred to as the
state.
Select one:
a. O and D
b. Oxygenated and Deoxygenated
c. Relaxed or R and Tense or T Correct! Oxygen binding causes a marked change in hemoglobin
structure. In the presence of oxygen, hemoglobin is in the Relaxed state or R state. In the absence
of oxygen, hemoglobin is in the Tense state or T state.
d. There is no difference between the two states
Patients with sickle cell anemia have atypical hemoglobin, which will distort the red blood cells into
sickle shape during oxygen delivery. The substitution of a hydrophilic amino acid with a
amino acid in hemoglobin subunits results in the polymerization of hemoglobin, leading
to the sickling of red blood cells.
Select one:
a. hydrophobic Correct! In case of sickle cell anemia, a hydrophilic amino acid-glutamate is replaced
by a non polar-hydrophobic amino acid-valine, leading to polymerization of hemoglobin, fibril
formation and eventually sickling of the red blood cells.
b. cysteine
c. polar
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, d. hydrophilic
Hemglobin consists of four proteins subunits. Each subunit contains a heme group that holds an iron
atom, which can bind to an oxygen molecule.
When binding hemoglobin or myoglobin, CO binds in place of .
Select one:
a. Iron
b. Oxygen Correct! CO binds in place of oxygen.
c. Histidine
d. Heme
Structurally, hemoglobin can bind molecules of oxygen, all of which could potentially be replaced by
carbon monoxide.
Select one:
a. 4 Correct!
b. 2
c. 1
d. 3
Carbon monoxide outcompetes oxygen for attachment to the group of hemoglobin where it
is permanently, covalently attached.
Select one:
a. histidine
b. sulfide
c. ligand
d. heme Correct
As carbon monoxide binds to hemoglobin, the protein subunits change conformation to allow
carbon monoxide to bind faster. This process is called .
Select one:
a. positive cooperativity Correct! Binding of one carbon monoxide molecule changes the
conformation of the hemoglobin in a fashion such that more molecules of carbon monoxide can bind to
the same protein.
b. competitive inhibition
c. non-competitive inhibition
d. allosteric binding
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oxygen storage and delivery capabilities. How many subunits do myoglobin and hemoglobin each have?
Select one:
a. Two, Three
b. One, Two
c. One, Four Correct! Myoglobin consist of one and hemoglobin consists of four subunits. The
number of subunits affects their respective oxygen storage and delivery capabilities.
d. Four, One
Addition of alters the shape of the iron–heme complex, and therefore its
absorption of light as indicated by its color change from dark purple (the color of hemoglobin in
venous blood) to brilliant scarlet (the color of hemoglobin in arterial blood).
Select one:
a. iron
b. oxygen Correct!
c. globin subunit
d. porphyrin
Oxygen binding alters the structure of an entire hemoglobin tetramer, so the structures of oxyhemoglobin
and deoxyhemoglobin are noticeably different. The oxyhemoglobin conformation is specifically referred
to as the state, whereas the deoxyhemoglobin conformation is referred to as the
state.
Select one:
a. O and D
b. Oxygenated and Deoxygenated
c. Relaxed or R and Tense or T Correct! Oxygen binding causes a marked change in hemoglobin
structure. In the presence of oxygen, hemoglobin is in the Relaxed state or R state. In the absence
of oxygen, hemoglobin is in the Tense state or T state.
d. There is no difference between the two states
Patients with sickle cell anemia have atypical hemoglobin, which will distort the red blood cells into
sickle shape during oxygen delivery. The substitution of a hydrophilic amino acid with a
amino acid in hemoglobin subunits results in the polymerization of hemoglobin, leading
to the sickling of red blood cells.
Select one:
a. hydrophobic Correct! In case of sickle cell anemia, a hydrophilic amino acid-glutamate is replaced
by a non polar-hydrophobic amino acid-valine, leading to polymerization of hemoglobin, fibril
formation and eventually sickling of the red blood cells.
b. cysteine
c. polar
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https://www.coursehero.com/file/26662459/Biochemistry-Module-3docx/
, d. hydrophilic
Hemglobin consists of four proteins subunits. Each subunit contains a heme group that holds an iron
atom, which can bind to an oxygen molecule.
When binding hemoglobin or myoglobin, CO binds in place of .
Select one:
a. Iron
b. Oxygen Correct! CO binds in place of oxygen.
c. Histidine
d. Heme
Structurally, hemoglobin can bind molecules of oxygen, all of which could potentially be replaced by
carbon monoxide.
Select one:
a. 4 Correct!
b. 2
c. 1
d. 3
Carbon monoxide outcompetes oxygen for attachment to the group of hemoglobin where it
is permanently, covalently attached.
Select one:
a. histidine
b. sulfide
c. ligand
d. heme Correct
As carbon monoxide binds to hemoglobin, the protein subunits change conformation to allow
carbon monoxide to bind faster. This process is called .
Select one:
a. positive cooperativity Correct! Binding of one carbon monoxide molecule changes the
conformation of the hemoglobin in a fashion such that more molecules of carbon monoxide can bind to
the same protein.
b. competitive inhibition
c. non-competitive inhibition
d. allosteric binding
This study source was downloaded by 100000829878664 from CourseHero.com on 07-29-2022 01:08:00 GMT -05:00
https://www.coursehero.com/file/26662459/Biochemistry-Module-3docx/
