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Chapter 7 Hemoglobin

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Chapter 7
Amy Arce
Quiz por Amy Arce, atualizado more than 1 year ago
Amy Arce
Criado por Amy Arce mais de 8 anos atrás
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Resumo de Recurso

Questão 1

Questão
Hemoglobin is a
Responda
  • 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

Questão 2

Questão
Myoglobin
Responda
  • 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

Questão 3

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

Questão 4

Questão
The heme group consist of
Responda
  • 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

Questão 5

Questão
The iron lies in the middle of the protoporphyrin bound to three nitrogens
Responda
  • True
  • False

Questão 6

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

Questão 7

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

Questão 8

Questão
The [blank_start]sixth[blank_end] coordination site binds [blank_start]oxygen[blank_end]
Responda
  • sixth
  • oxygen

Questão 9

Questão
The structure of myoglobin prevents the release of reactive oxygen species
Responda
  • True
  • False

Questão 10

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

Questão 11

Questão
Heme with Fe3+
Responda
  • does not bind oxygen
  • does bind oxygen

Questão 12

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

Questão 13

Questão
The distal histidine of myoglobin prevents the release of
Responda
  • Fe3+
  • O2-
  • Fe
  • O2

Questão 14

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

Questão 15

Questão
Myoglobin consist of
Responda
  • 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

Questão 16

Questão
Hemoglobin consist of
Responda
  • Four chains
  • 2 identical α chains
  • 4 identical α chains
  • 2 identical β chains.
  • 4 identical β chains.

Questão 17

Questão
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
Responda
  • globin

Questão 18

Questão
Hemoglobin binds oxygen cooperatively
Responda
  • True
  • False

Questão 19

Questão
[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]
Responda
  • Myoglobin
  • Hemoglobin
  • hyperbolic
  • sigmoid
  • hemoglobin
  • myoglobin
  • sigmoid
  • hyperbolic
  • cooperative
  • non-cooperative

Questão 20

Questão
Hemoglobin is not effective in providing oxygen to exercising tissue
Responda
  • True
  • False

Questão 21

Questão
Because of cooperatively between O2 binding sites,
Responda
  • 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

Questão 22

Questão
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].
Responda
  • T state
  • R state
  • R state
  • T state

Questão 23

Questão
R state
Responda
  • relaxed state
  • tight state
  • binding of oxygen
  • facilitates the release of oxygen

Questão 24

Questão
T state
Responda
  • Tight state
  • Relaxed state
  • binding of oxygen
  • facilitates the release of oxygen

Questão 25

Questão
R state has a greater affinity for oxygen than does the T state
Responda
  • True
  • False

Questão 26

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

Questão 27

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

Questão 28

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

Questão 29

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

Questão 30

Questão
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.
Responda
  • T state
  • R state
  • release
  • binding

Questão 31

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

Questão 32

Questão
In fetal hemoglobin,
Responda
  • 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

Questão 33

Questão
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.
Responda
  • True
  • False

Questão 34

Questão
Bohr effect
Responda
  • 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

Questão 35

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

Questão 36

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

Questão 37

Questão
Sickle cell anemia results from the aggregation of mutated deoxyhemoglobin molecules
Responda
  • 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.

Questão 38

Questão
Thalassemia
Responda
  • 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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