Chapter 7 Hemoglobin

Question 1 of 38

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Hemoglobin is a

Select one or more of the following:

  • 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 of 38

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Myoglobin

Select one of the following:

  • 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 of 38

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The ability of myoglobin and hemoglobin to bind oxygen depends on the presence of a heme group

Select one of the following:

  • True
  • False

Question 4 of 38

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The heme group consist of

Select one of the following:

  • 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 of 38

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The iron lies in the middle of the protoporphyrin bound to three nitrogens

Select one of the following:

  • True
  • False

Question 6 of 38

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Iron can from two additional bonds, at the ( fifth, second, fourth ) and ( sixth, third, fifth ) coordination sites

Question 7 of 38

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The imidazole ring of a histidine called the proximal histidine is occupied by the

Select one of the following:

  • Fourth coordination

  • Fifth coordination

  • Sixth coordination

  • Seventh coordination

Question 8 of 38

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Fill the blank spaces to complete the text.

The coordination site binds

Question 9 of 38

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The structure of myoglobin prevents the release of reactive oxygen species

Select one of the following:

  • True
  • False

Question 10 of 38

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

Select one of the following:

  • True
  • False

Question 11 of 38

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Heme with Fe3+

Select one of the following:

  • does not bind oxygen

  • does bind oxygen

Question 12 of 38

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Myoglobin with iron in the Fe3+ state is called

Select one of the following:

  • metmyoglobin.

  • metamyoglobin

  • oxymyoglobin

  • deoxymyoglobin

Question 13 of 38

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The distal histidine of myoglobin prevents the release of

Select one of the following:

  • Fe3+

  • O2-

  • Fe

  • O2

Question 14 of 38

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A hydrogen bond donated by the distal histidine residue to the bound oxygen molecule helps stabilize oxymyoglobin

Select one of the following:

  • True
  • False

Question 15 of 38

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Myoglobin consist of

Select one of the following:

  • 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 of 38

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Hemoglobin consist of

Select one or more of the following:

  • Four chains

  • 2 identical α chains

  • 4 identical α chains

  • 2 identical β chains.

  • 4 identical β chains.

Question 17 of 38

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Many of the helices in each subunit are arranged in a pattern also found in myoglobin, a structure called the fold

Question 18 of 38

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Hemoglobin binds oxygen cooperatively

Select one of the following:

  • True
  • False

Question 19 of 38

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( Myoglobin, Hemoglobin ) displays a ( hyperbolic, sigmoid ) oxygen binding curve, while ( hemoglobin, myoglobin ) exhibits a ( sigmoid, hyperbolic ) curve, indication that O2 binding and release is ( cooperative, non-cooperative )

Question 20 of 38

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Hemoglobin is not effective in providing oxygen to exercising tissue

Select one of the following:

  • True
  • False

Question 21 of 38

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Because of cooperatively between O2 binding sites,

Select one of the following:

  • 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 of 38

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The quaternary structure of deoxyhemoglobin is referred to as the ( T state, R state ), while that of oxyhemoglobin is the ( R state, T state ).

Question 23 of 38

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R state

Select one or more of the following:

  • relaxed state

  • tight state

  • binding of oxygen

  • facilitates the release of oxygen

Question 24 of 38

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T state

Select one or more of the following:

  • Tight state

  • Relaxed state

  • binding of oxygen

  • facilitates the release of oxygen

Question 25 of 38

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R state has a greater affinity for oxygen than does the T state

Select one of the following:

  • True
  • False

Question 26 of 38

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It is sequential in that in hemoglobin with one O2 bound,

Select one of the following:

  • the remaining subunits are in the T state.

  • the remaining subunits are in the R state.

Question 27 of 38

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It is concerted in that in hemoglobin with three O2 bound,

Select one of the following:

  • the remaining subunit is in the R state

  • the remaining subunit is in the T state

Question 28 of 38

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The transition from deoxyhemoglobin (T state) to oxyhemoglobin (R state) occurs upon oxygen binding.

Select one of the following:

  • True
  • False

Question 29 of 38

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2,3 Bisphosphoglycerate in red cells is crucial in determining the oxygen affinity of myoglobin

Select one of the following:

  • True
  • False

Question 30 of 38

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2, 3-Bisphosphoglycerate (2,3-BPG) stabilizes the ( T state, R state ) of hemoglobin and thus facilitates the ( release, binding ) of oxygen.

Question 31 of 38

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

Select one of the following:

  • True
  • False

Question 32 of 38

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In fetal hemoglobin,

Select one or more of the following:

  • 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 of 38

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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.

Select one of the following:

  • True
  • False

Question 34 of 38

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Bohr effect

Select one of the following:

  • 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 of 38

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Most carbon dioxide is carried to the lungs in the blood as bicarbonate ion.

Select one of the following:

  • True
  • False

Question 36 of 38

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Carbonic acid dissociates to form HCO3- and H+ resulting in a rise in pH inside the cell

Select one of the following:

  • True
  • False

Question 37 of 38

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Sickle cell anemia results from the aggregation of mutated deoxyhemoglobin molecules

Select one or more of the following:

  • 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 of 38

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Thalassemia

Select one or more of the following:

  • 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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Chapter 7 Hemoglobin

Amy Arce
Quiz by , created about 1 year ago

Chapter 7

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Amy Arce
Created by Amy Arce about 1 year ago
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