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BMS > Hemoglobin and Hemoglobinopathies > Flashcards

Hemoglobin and Hemoglobinopathies Flashcards

1
Q

Is like a little computer, sensing the gasses around it, the pH around it, and the other ligands in the area. Then it computes wether or not it needs to release or bind oxygen

A

Hemoglobin

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2
Q

Goes through a breathing motion. As it breathes, it binds an oxygen molecule. Then when it reaches it’s destination, it exhales its oxygen and inhales CO2

A

Hemoglobin

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3
Q

Per fluorocarbons make liquids at room temperature with very high solubility for gasses such as oxygen. When blood is replaced with this liquid, a rat can breathe in water or in air. This is called

A

Liquid ventillation

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4
Q

A non amino acid type group

A

Cofactor

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5
Q

Acts as a dissolver of oxygen

A

Heme

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6
Q

Heme needs to be in blood because by itself, heme is oxidized forming a

A

u-bridged heme compound with a hyrdrophobic layer on the top and bottom, which will cause them to aggregate out of solution

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7
Q

Two ferrous (2+) hemes can form a bridged complex with oxygen, producing

A

Non-functional oxidized heme

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8
Q

What do we call reduced Fe 2+ hemoglobin?

A

Ferrohemoglobin (an oxygen carrier)

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9
Q

What do we call oxidized Fe 3+ hemoglobin?

A

Methemoglobin (nonfunctional)

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10
Q

Hemoglobin is only functional in the

A

Ferrous state (2+)

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11
Q

What is a synthetic way to make heme and keep it from forming bridged heme aggregates?

-developed for artificial blood substitutes

A

Picket-fence heme

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12
Q

In the cell, our hemoglobin is not the picket-fence type. So how do we protect heme from being oxidized?

A

Heme is surrounded by the hemoglobin protein, which prevents oxidation and u-bridge formation

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13
Q

Heme is the O2 binding molecule common to

A

Myoglobin and Hemoglobin

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14
Q

Once sequestered inside a hydrophobic pocket created by the folded globin polypeptide, heme encounters a protective environment that minimizes

A

The oxidation of Fe 2+ to Fe 3+

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15
Q

Mutations that lead to anemia do so by weakening the proteins binding to heme, thus making it more likely that

A

Iron is oxidized, creating nonfunctional methemoglobin

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16
Q

The O2 binding of myoglobin is not optimal for

A

O2 transport

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17
Q

Which binds oxygen more tightly, myoglobin or hemoglobin?

A

Myoglobin

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18
Q

Enables hemoglobin to deliver oxygen over a range that best suits our needs

A

Hemoglobins complex structure

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19
Q

The partial pressure of oxygen, where protein sites are half saturated

A

P50

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20
Q

Oxygenated and deoxygenated blood are different colors because

A

They absorb at different wavelengths

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21
Q

Measures the absorption of 660nm and 940nm wavelengths in the arteries

A

Pulse oximetry

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22
Q

If we take ratios of the extinction coefficients at 660nm and 940 nm, what does it mean if the ratio is less than one?

A

We have more oxygenated blood than deoxygenated blood

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23
Q

A single-chain globular protein of 153 amino acids.

-made up of all alpha helices

A

Myoglobin

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24
Q

Myoglobin is located in the

A

Cytosol of muscle cells

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25
Q

Binds oxygen that has been released by Hb in the tissue capillaries and has subsequently diffused across cellular membranes

A

Myoglobin

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26
Q

Controls the gasses which can and can not bind heme

-Prevents CO from binding

A

The E-helix Histidine

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27
Q

What holds myoglobin together?

A

The hydrophobic effect from the 60 hydrophobic residues

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28
Q

How many circulating globins are there?

A

1 (hemoglobin)

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29
Q

How many non-circulating globins are there?

A

3 (myoglobin, neuroglobin, cytoglobin)

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30
Q

Hemoglobin is essentially four myoglobin subunits coming together. These four subunits interact with eachother and change the

A

P50

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31
Q

A different globin gene encodes

A

the alpha and beta subunits

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32
Q

The primary sequence of hemoglobin and myoglobin is actually

A

Much different (but their structures are almost identical)

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33
Q

What holds hemoglobin together?

A

Intermolecular salt bridges (ex: btw Asp and Lys)

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34
Q

Why are the intermolecular salt bridges that hold hemoglobin together good?

A
  1. ) They don’t compete with the hydrophobic interactions in the core
  2. ) They allow for flexibility
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35
Q

The amount of oxygen bound to hemoglobin by the time it reaches the tissues is

A

Low

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36
Q

Allows us to sequester more oxygen within the blood

A

Hemoglobin

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37
Q

Takes more partial pressure of oxygen to 50% saturate

A

Hemoglobin

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38
Q

Ligand binding causes structural rearrangement that
orients enzyme in its active conformation and makes it
easier for next substrates to bind. This describes

A

Cooperative binding

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39
Q

Also utilized in protein folding. Once the fold starts, it becomes a chain reaction of folding

A

Cooperativity

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40
Q

When you look at oxygen binding, we are essentially moving from a low affinity state to a high affinity state.
Hemoglobin is in a low affinity state, then the first oxygen binds and

A

The affinity increases and keeps increasing with each successive oxygen that binds

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41
Q

A measure of the degree of cooperativity

-represented by n in the saturation equation

A

Hill coefficient

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42
Q

Hemoglobins high degree of cooperativity enables it to

A

Pick up more oxygen in the lungs and deliver more oxygen in the body

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43
Q

Favors the T-state

A

Deoxy-Hb

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44
Q

Favors the R-state

A

Oxy-Hb

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45
Q

The binding of oxygen to a hemoglobin subunit in the T-state triggers a change in conformation to the

A

R state

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46
Q

When the entire protein undergoes the T to R transition, the αβ subunit pairs slide past eachother and rotate, which

A

Narrows the pocket between the β subunits

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47
Q

Change little in the transition from the T state to the R state

A

The structures of the individual α and β subunits

48
Q

A protein that exhibits changes in ligand (or substrate) affinity under the influence of small molecule

A

Allosteric Protein

49
Q

Bind to proteins at sites that are spatially distinct from the active sites and, through long-range conformational change, alter the affinity of the active site for the substrate

A

Allosteric Effectors

50
Q

Often multi-subunit proteins

A

Allosteric proteins

51
Q

May either increase an enzymes affinity for substrate or decrease an enzymes affinity for substrate

A

Allosteric effector

52
Q

What are the two major conformation of hemoglobin?

A

T and R states

53
Q

Although oxygen binds to hemoglobin in either state, it has a significantly higher affinity for hemoglobin in the

54
Q

More stable when oxygen is absent experimentally and is thus the predominant conformation of deoxyhemoglobin

55
Q

What makes the T-state more tense than the R state?

A

The T state has an increased number of salt bridges

56
Q

Describes how hydrogen ions and carbon dioxide effect the affinity of oxygen in hemoglobin

A

Bohr Effect

57
Q

What is the effect on hemoglobin of lowering pH?

A

When hemoglobin binds oxygen, it releases hydrogen ions. However, at lower pH, there are more hydrogen ions in solution, which prevents hemoglobin from binding oxygen as well. Thus the affinity of hemoglobin for oxygen is lower in acidic pH

58
Q

What is the effect on hemoglobin of increases pH?

A

Higher pH increases the affinity of hemoglobin for oxygen. It will bind oxygen more tightly

59
Q

What effect do high levels of carbon dioxide have on hemoglobins affinity for oxygen?

A

High levels of CO2 result in the formation of carbonic acid, which decreases pH, thereby decreasing Hb’s affinity for oxygen

60
Q

What effect do low levels of carbon dioxide have on hemoglobins affinity for oxygen?

A

Low levels of CO2 increase Hb’s affinity for oxygen

61
Q

What serves as the pH sensor on Hb?

A

Asp 94 and His 146 on the β chains far from heme binding sites

62
Q

Why is the T state favored at lower pH?

A

His 146β gets protonated and becomes positively charged, resulting in salt bridge formation with Asp 94β. This interaction stabilizes the T state

63
Q

Why is the R state favored at higher pH?

A

Histidine 146β is deprotonated, breaking the salt bridge with Asp 94β, thus relaxing the protein and stabilizing the R state

64
Q

In the lungs, Hb releases a proton as it binds O2, the proton reacts with bicarbonate, reforming carbonic acid. This results in

A

CO2 liberation and water formation

65
Q

Some CO2 is transported directly with Hb by forming

A

Carbamates with amine groups on the N-terminus

66
Q

When hemoglobin goes from the R state to the T state, two free amines are exposed. The amines can bind CO2, forming a carbonate. This stabilizes the

67
Q

Promotes the excretion of bicarbonate in the kidneys

A

Diamox (acetazolamide)

68
Q

How can we use Diamox (acetazolamide) to treat altitude sickness, which is caused by a decrease in oxygenation of the bodies tissues at high altitudes.

A

When bicarbonate is excreted in the kidneys, blood pH drops. This drop in blood pH decreases the affinity of hemoglobin for oxygen, which improves Hb’s ability to deliver oxygen to the body

69
Q

Binds to the R state of Hb directly on the heme iron, as well as a thiol-nitrosyl bond on Cys 93β

A

Nitric oxide

70
Q

Release of Nitric oxide upon deoxygenation of Hb allows NO to?

A

Bind vascular endothelium receptors, triggering vasodilation and increased blood flow to hypoxic tissues

71
Q

A normal product of glycolysis in erythrocytes that is critical to the release of oxygen from hemoglobin

72
Q

Binding of 2,3-Biphosphoglycerate (2,3-BPG) to Hb does what?

A

Stabilizes the T state and reduces affinity for oxygen

73
Q

Without 2,3-BPG, hemoglobin acts just like

74
Q

What affect does acidification of blood have on myoglobin?

75
Q

How does 2,3-BPG stabilize the T-state and reduce hemoglobins affinity for oxygen?

A

Forms a network of salt bridges between the two β subunits

76
Q

What three things stabilize the T-state?

-decreases Hb’s affinity for oxygen?

A
  1. ) Low pH
  2. ) 2,3, BPG
  3. ) High levels of CO2
77
Q

What three things stabilize the R-state?

-Increases Hb’s affinity for oxygen

A
  1. ) High pH
  2. ) Oxygen (allostery)
  3. ) Nitric oxide
78
Q

The varying Hb’s are arranged on chromosomes in the order of

A

Their expression during development

79
Q

Instead of being composed of 2α and 2β subunits, fetal hemoglobin is composed of

A

2α and 2ƴ subunits

80
Q

Has a lower affinity for 2,3-BPG

-Has a higher affinity for oxygen

81
Q

There are two very important Histidine’s in Hb. The distal histidine binds the Fe 2+. What does the other (known as the E helix) do?

A

Sits on the top side of the Fe 2+ and destabilizes CO binding while at the same time stabilizes oxygen binding

82
Q

A colorless, odorless gas responsible for more than half of annual poisoning deaths worldwide

A

Carbon Monoxide (CO)

83
Q

How much greater of an affinity does CO have for Hb than oxygen?

84
Q

Produces cherry red discoloration of the skin and organs

-treated with 100% or hyperbaric oxygen

A

CO poisoning

85
Q

Glucose can be added to the N-terminal of the beta chains of Hb, resulting in

A

Glycation of Hb by glucose to HbA1c

86
Q

Glycation of Hb by glucose to HbA1c is a relatively irreversible reaction which affects the binding of

87
Q

Representative of glucose over 6-8 weeks, making them a good indicator of diabetes risk or the efficacy of current treatment

A

HbA1c levels

88
Q

Affects the electrophoretic mobility of Hb

A

Glycosylation

89
Q

When Hb sickles it can cause red blood cells to rupture, which can result in

A

Blockages and Ischemia

90
Q

In people with Sickle Cell Anemia, Red blood cells are more

A

Fragile than normal

91
Q

An autozomal recessive (AR) disorder that is a homozygous condition

A

Sickle Cell Anemia

92
Q

You can be heterozygous for sickle cell and not have full blown sickle cell anemia. This is called having the

A

Sickle Cell Trait

93
Q

Usually asymptomatic, except in the renal medulla where oxygen tensions are low enough to induce sickling and renal damage

A

Sickle cell trait

94
Q

Butyrate and hydroxyurea stimulate the production of HbF, why might this be an effective treatment to alleviate the presentation of sickle cell?

A

HbF brings in healthy beta chains in the form of Y chains

95
Q

What are two other methods to treat sickle cell?

A
  1. ) Bone marrow stem cell transplant

2. ) Gene therapy

96
Q

Individuals heterozygous for sickle cell are protected against the most lethal forms of

97
Q

Part of the life cycle of the malaria parasite plasmodium is spent reproducing in red blood cells, however, free Hb is toxic to plasmodium so it sequesters Hb into a crystalline form called

98
Q

Many anti-malarials disrupt

A

Hemozoin formation

99
Q

Infection of RBCs by plasmodium triggers sickling, recruiting phagocytes that then clear the infected cells in

100
Q

A Glu 6 Lys mutation that causes intracellular crystallization of Hb and cation leak, resulting in dehydration

A

Hemozoin (HbC)

101
Q

Genetic disorders of Hb synthesis

A

Thalassemias

102
Q

What are the three main causes of Thalassemias?

A
  1. ) Hb gene is missing
  2. ) Gene is present, but expression is impaired
  3. ) mRNA is produced, but it encodes disfunctional Hb
103
Q

Thalassemias caused by impaired expression of the Hb gene are due to

A

Modifications to gene promoter region

104
Q

What causes the Thalassemias where the mRNA is produced but it encodes grossly disfunctional Hb?

A

Introduction of an early stop codon

105
Q

In β-thalassemias, α-chains aggregate into

A

Heinz bodies

106
Q

The β4 tetramers form (HbH) which has reduced

solubility and lacks allosteric regulation found in HbA

A

α-thalassemias

107
Q

What are the four types of α-thalassemias

A
  1. ) Silent carrier
  2. ) Trait
  3. ) Disease
  4. ) Hydrops fetalis (death occur because no alpha chains)
108
Q

β-thalassemias have higher levels of

A

HbF or HbA2

109
Q

α-thalassemias have higher levels of

A

Hb Barts: y4, or HbH

110
Q

The nonfunctional oxidized version of hemoglobin

-often manifests in cyanosis (blue lips, extremities)

A

Methemoglobin

111
Q

Higher than noirmal (> 1%) levels of oxidized hemoglobin

A

Methemoglobinemia

112
Q

Methemoglobinemia can be induced by certain

A

Antibiotics

113
Q

Effects interactions with cytochrome-b5-reductase and can lead to methemoglobinemia

A

HbM (Hb Hyde Park) mutations

114
Q

Can be used to treat cyanide poisoning by oxidizing Hb, which readily binds cyanide, producing cyanohemoglobin.

A

Amyl Nitrate

115
Q

The production of cyanohemoglobin keeps HCN from binding

-Critical for respiration

A

Cytochrome C oxidase

BMS (62 decks)

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