Hemoglobin and Myoglobin Flashcards

1
Q

Hemeprotein

A

proteins with heme as tightly bound prosthetic group

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2
Q

Prosthetic Group

A

coenzyme permanently associated with enzyme or protein

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3
Q

Cytochromes

A

heme group serves as electron carrier that can be oxidized and reduced
in ETC

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4
Q

Catalase

A

heme is part of active site of enzyme that catalyzes breakdown of hydrogen peroxide
in peroxisomes

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5
Q

Heme use in Myoglobin and Hemoglobin

A

heme used to reversibly bind oxygen

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6
Q

Heme Structure

A

iron in center of porphyrin ring

makes 6 bonds- 4 to iron, 1 to R group of histidine of globin, 1 to oxygen

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7
Q

Myoglobin

A

in heart and skeletal m

O reservoir; carrier that increases transport rate w/in muscle cells

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8
Q

Hemoglobin

A

Red Blood Cells
transports 4 O2 mol from lungs to capillaries of tissues
transports CO2 and H from tissues to lungs

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9
Q

T Form

A

deoxy form when no O bound

low O affinity

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10
Q

R Form

A

O binding causes break of some polar bonds of T form

high O affinity

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11
Q

O binding myoglobin vs hemoglobin

A

1 O to Myoglobin
4 O to Hemoglobin
Myoglobin has higher affinity

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12
Q

Bohr Effect

A

Decreases O affinity at lower pH
shifts curve to right
stabilizes T form

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13
Q

2,3 BPG

A

stabilizes T form
decreases O affinity
shifts curve right

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14
Q

CO2 Binding

A

stabilizes T form
less O affinity
shifts curve right

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15
Q

CO Binding

A

hemoglobin has higher affinity for CO than O; binds more closely
higher O affinity
R form
Shifts curve left

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16
Q

Fetal Hemoglobin

HbF

A

lower affinity for 2,3 BPG (missing some + aa in beta chains of 2,3 BPG)
higher O affinity
shifts curve left
Stabilizes R form

17
Q

What are the proton sources that decrease pH so the Bohr effect can take place?

A

acids made by tissues (lactic acid)

high levels of CO2 at peripheral tissues (carbonic acids and bicarbonate)

18
Q

pH gradient between lungs and tissues

A

CO2 releasing carbonic acids and bicarbonate from tissues makes a higher pH in lungs and lower at tissues
hemoglobin becomes more efficient oxygen transporter

19
Q

Mechanism of the Bohr Effect

A

Deoxyhemoglobin has a higher affinity for protons than oxyhemoglobin (histidine R groups have higher pKa when not O bound)
become protonated = charged R group
charged group form stronger ionic interactions- lower O affininity

20
Q

Where does 2,3-BPG effect take place?

A

high concentrations of RBC

binds only to deoxyhemoglobin- decreases O affinity

21
Q

Mechanism of 2,3- BPG

A
binds in pocket between 2 beta globin chains in deoxyhemoglobin
chains contain (+) aa that bind (-) 2,3- BPG
O binding = BPG removed
22
Q

Response of 2,3- BPG to anemia/ chronic hypoxia

A

2,3-BPG levels rise

increases ability to unload O in tissues

23
Q

Role of 2,3- BPG in transfused blood

A

needed for normal transport
w/o O can not be unloaded efficiently
BPG lost when blood is stored; O binds too tightly in transfused patients until BPG levels return to normal

24
Q

Transporting forms of CO2

A

Normal- bicarbonate ion

Or- carbamate bound to N terminal aa of hemoglobin which forms carbaminohemoglobin

25
Q

Where does CO2 dissociate from hemoglobin?

A

Lungs

26
Q

Affect of CO binding to hemoglobin

A
tight binding (200x higher affinity)
No O can unload at peripheral tissues
27
Q

Effects of fetal hemoglobin

A

higher O affinity

able to absorb O from maternal circulation across placenta

28
Q

Hemoglobin A2

A

minor hemoglobin with unknown function

29
Q

Sickle Cell Anemia

Hemoglobin S disease

A

Glutamate replaced by valine (more +)
RBC lifespan about 20 days
T form stiffens and distorts cell
can interrupt flow through capillaries- anoxia- can kill tissue

30
Q

Hemoglobin C Disease

A

Lysine substituted for glutamate

homozygotes have mild chronic hemolytic anemia

31
Q

Hemoglobin SC Disease

A

genetics- 1 HbS and 1 HbC

some sickling and crises