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Chapter 7 Hemoglobin

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Chapter 7
Amy Arce
Quiz by Amy Arce, updated more than 1 year ago
Amy Arce
Created by Amy Arce about 9 years ago
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Resource summary

Question 1

Question
Hemoglobin is a
Answer
  • red blood cell protein that transports oxygen via its four heme-bound subunits from the lungs to the tissues
  • Gives blood its red color
  • allosteric protein
  • Quaternary structure
  • Tertiary structure
  • if abnormal in primary structure can lead to diseases or mutations such as sickle cell
  • bind of oxygen is not cooperative

Question 2

Question
Myoglobin
Answer
  • binds oxygen in muscle cells
  • displays cooperatively in oxygen binding and release
  • is a quaternary structure
  • can lead to sickle cell disease if abnormalities exist in primary structure

Question 3

Question
The ability of myoglobin and hemoglobin to bind oxygen depends on the presence of a heme group
Answer
  • True
  • False

Question 4

Question
The heme group consist of
Answer
  • inorganic component called protoporphyrin and a central iron ion in the ferrous form, the only form that can bind oxygen
  • organic component called protoporphyrin and a central iron ion in the ferrous form, the only form that can bind oxygen
  • inorganic component called protoporphyrin and a central iron ion in the ferrous form, one out of many forms that can bind oxygen
  • organic component called protoporphyrin and a central iron ion in the ferrous form, one out of many forms that can bind oxygen

Question 5

Question
The iron lies in the middle of the protoporphyrin bound to three nitrogens
Answer
  • True
  • False

Question 6

Question
Iron can from two additional bonds, at the [blank_start]fifth[blank_end] and [blank_start]sixth[blank_end] coordination sites
Answer
  • fifth
  • second
  • fourth
  • sixth
  • third
  • fifth

Question 7

Question
The imidazole ring of a histidine called the proximal histidine is occupied by the
Answer
  • Fourth coordination
  • Fifth coordination
  • Sixth coordination
  • Seventh coordination

Question 8

Question
The [blank_start]sixth[blank_end] coordination site binds [blank_start]oxygen[blank_end]
Answer
  • sixth
  • oxygen

Question 9

Question
The structure of myoglobin prevents the release of reactive oxygen species
Answer
  • True
  • False

Question 10

Question
Superoxide is very reactive, and should it leave the heme, ferric iron (Fe3+) would result.
Answer
  • True
  • False

Question 11

Question
Heme with Fe3+
Answer
  • does not bind oxygen
  • does bind oxygen

Question 12

Question
Myoglobin with iron in the Fe3+ state is called
Answer
  • metmyoglobin.
  • metamyoglobin
  • oxymyoglobin
  • deoxymyoglobin

Question 13

Question
The distal histidine of myoglobin prevents the release of
Answer
  • Fe3+
  • O2-
  • Fe
  • O2

Question 14

Question
A hydrogen bond donated by the distal histidine residue to the bound oxygen molecule helps stabilize oxymyoglobin
Answer
  • True
  • False

Question 15

Question
Myoglobin consist of
Answer
  • a single polypeptide chain, formed of α- helices connected by turns, with one oxygen binding site
  • a multiple polypeptide chains, formed of α- helices connected by turns, with one oxygen binding site
  • a multiple polypeptide chains, formed of β- helices connected by turns, with one oxygen binding site
  • a single polypeptide chain, formed of β- helices connected by turns, with one oxygen binding site

Question 16

Question
Hemoglobin consist of
Answer
  • Four chains
  • 2 identical α chains
  • 4 identical α chains
  • 2 identical β chains.
  • 4 identical β chains.

Question 17

Question
Many of the helices in each subunit are arranged in a pattern also found in myoglobin, a structure called the [blank_start]globin[blank_end] fold
Answer
  • globin

Question 18

Question
Hemoglobin binds oxygen cooperatively
Answer
  • True
  • False

Question 19

Question
[blank_start]Myoglobin[blank_end] displays a [blank_start]hyperbolic[blank_end] oxygen binding curve, while [blank_start]hemoglobin[blank_end] exhibits a [blank_start]sigmoid[blank_end] curve, indication that O2 binding and release is [blank_start]cooperative[blank_end]
Answer
  • Myoglobin
  • Hemoglobin
  • hyperbolic
  • sigmoid
  • hemoglobin
  • myoglobin
  • sigmoid
  • hyperbolic
  • cooperative
  • non-cooperative

Question 20

Question
Hemoglobin is not effective in providing oxygen to exercising tissue
Answer
  • True
  • False

Question 21

Question
Because of cooperatively between O2 binding sites,
Answer
  • hemoglobin delivers more O2 to actively metabolizing tissues than would myoglobin or any noncooperative protein, even one with optimal O2 affinity
  • hemoglobin delivers more O2 to actively metabolizing tissues than would myoglobin or any cooperative protein, even one with optimal O2 affinity
  • myoglobin delivers more O2 to actively metabolizing tissues than would hemoglobin or any noncooperative protein, even one with optimal O2 affinity

Question 22

Question
The quaternary structure of deoxyhemoglobin is referred to as the [blank_start]T state[blank_end], while that of oxyhemoglobin is the [blank_start]R state[blank_end].
Answer
  • T state
  • R state
  • R state
  • T state

Question 23

Question
R state
Answer
  • relaxed state
  • tight state
  • binding of oxygen
  • facilitates the release of oxygen

Question 24

Question
T state
Answer
  • Tight state
  • Relaxed state
  • binding of oxygen
  • facilitates the release of oxygen

Question 25

Question
R state has a greater affinity for oxygen than does the T state
Answer
  • True
  • False

Question 26

Question
It is sequential in that in hemoglobin with one O2 bound,
Answer
  • the remaining subunits are in the T state.
  • the remaining subunits are in the R state.

Question 27

Question
It is concerted in that in hemoglobin with three O2 bound,
Answer
  • the remaining subunit is in the R state
  • the remaining subunit is in the T state

Question 28

Question
The transition from deoxyhemoglobin (T state) to oxyhemoglobin (R state) occurs upon oxygen binding.
Answer
  • True
  • False

Question 29

Question
2,3 Bisphosphoglycerate in red cells is crucial in determining the oxygen affinity of myoglobin
Answer
  • True
  • False

Question 30

Question
2, 3-Bisphosphoglycerate (2,3-BPG) stabilizes the [blank_start]T state[blank_end] of hemoglobin and thus facilitates the [blank_start]release[blank_end] of oxygen.
Answer
  • T state
  • R state
  • release
  • binding

Question 31

Question
2. 2, 3-BPG binds to a pocket in the hemoglobin tetramer that exists only when hemoglobin is in the R state.
Answer
  • True
  • False

Question 32

Question
In fetal hemoglobin,
Answer
  • the β chain is replaced with a γ chain
  • The fetal α2γ2 hemoglobin does not bind 2, 3-BPG as well as adult hemoglobin does.
  • The reduced affinity for 2, 3-BPG results in fetal hemoglobin having a higher affinity for oxygen, binding oxygen when the mother’s hemoglobin is releasing oxygen

Question 33

Question
Carbon monoxide binds so tightly to iron of hemoglobin that it stabilizes the R state (binding of oxygen) to such a degree that the R to T transition does not occur.
Answer
  • True
  • False

Question 34

Question
Bohr effect
Answer
  • The stimulation of oxygen release (R state) by carbon dioxide and Hydrogen ions
  • The stimulation of oxygen release (T state) by carbon dioxide and Hydrogen ions

Question 35

Question
Most carbon dioxide is carried to the lungs in the blood as bicarbonate ion.
Answer
  • True
  • False

Question 36

Question
Carbonic acid dissociates to form HCO3- and H+ resulting in a rise in pH inside the cell
Answer
  • True
  • False

Question 37

Question
Sickle cell anemia results from the aggregation of mutated deoxyhemoglobin molecules
Answer
  • is a genetic disease caused by a mutation resulting in the substitution of valine for glutamate at position 6 of the β chains.
  • can be fatal when both alleles of the β chain are mutated.
  • trait offers some protection from malaria
  • one allele is mutated and one is normal such individuals are asymptomatic.

Question 38

Question
Thalassemia
Answer
  • caused by an imbalanced production of hemoglobin chains
  • another common genetic disorder of hemoglobin
  • another common genetic disorder of myoglobin
  • caused by the absence or underproduction of one of the hemoglobin chains
  • caused by the presence or overproduction of one of the hemoglobin chains
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