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Chapter 7 Hemoglobin

Beschreibung

Chapter 7
Amy Arce
Quiz von Amy Arce, aktualisiert more than 1 year ago
Amy Arce
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Zusammenfassung der Ressource

Frage 1

Frage
Hemoglobin is a
Antworten
  • 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

Frage 2

Frage
Myoglobin
Antworten
  • 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

Frage 3

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

Frage 4

Frage
The heme group consist of
Antworten
  • 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

Frage 5

Frage
The iron lies in the middle of the protoporphyrin bound to three nitrogens
Antworten
  • True
  • False

Frage 6

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

Frage 7

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

Frage 8

Frage
The [blank_start]sixth[blank_end] coordination site binds [blank_start]oxygen[blank_end]
Antworten
  • sixth
  • oxygen

Frage 9

Frage
The structure of myoglobin prevents the release of reactive oxygen species
Antworten
  • True
  • False

Frage 10

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

Frage 11

Frage
Heme with Fe3+
Antworten
  • does not bind oxygen
  • does bind oxygen

Frage 12

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

Frage 13

Frage
The distal histidine of myoglobin prevents the release of
Antworten
  • Fe3+
  • O2-
  • Fe
  • O2

Frage 14

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

Frage 15

Frage
Myoglobin consist of
Antworten
  • 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

Frage 16

Frage
Hemoglobin consist of
Antworten
  • Four chains
  • 2 identical α chains
  • 4 identical α chains
  • 2 identical β chains.
  • 4 identical β chains.

Frage 17

Frage
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
Antworten
  • globin

Frage 18

Frage
Hemoglobin binds oxygen cooperatively
Antworten
  • True
  • False

Frage 19

Frage
[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]
Antworten
  • Myoglobin
  • Hemoglobin
  • hyperbolic
  • sigmoid
  • hemoglobin
  • myoglobin
  • sigmoid
  • hyperbolic
  • cooperative
  • non-cooperative

Frage 20

Frage
Hemoglobin is not effective in providing oxygen to exercising tissue
Antworten
  • True
  • False

Frage 21

Frage
Because of cooperatively between O2 binding sites,
Antworten
  • 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

Frage 22

Frage
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].
Antworten
  • T state
  • R state
  • R state
  • T state

Frage 23

Frage
R state
Antworten
  • relaxed state
  • tight state
  • binding of oxygen
  • facilitates the release of oxygen

Frage 24

Frage
T state
Antworten
  • Tight state
  • Relaxed state
  • binding of oxygen
  • facilitates the release of oxygen

Frage 25

Frage
R state has a greater affinity for oxygen than does the T state
Antworten
  • True
  • False

Frage 26

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

Frage 27

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

Frage 28

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

Frage 29

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

Frage 30

Frage
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.
Antworten
  • T state
  • R state
  • release
  • binding

Frage 31

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

Frage 32

Frage
In fetal hemoglobin,
Antworten
  • 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

Frage 33

Frage
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.
Antworten
  • True
  • False

Frage 34

Frage
Bohr effect
Antworten
  • 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

Frage 35

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

Frage 36

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

Frage 37

Frage
Sickle cell anemia results from the aggregation of mutated deoxyhemoglobin molecules
Antworten
  • 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.

Frage 38

Frage
Thalassemia
Antworten
  • 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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