Hemoglobin Flashcards

1
Q

final enzyme of electron transport

A

cytochrome oxidase - O2 is reduced to H2O

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2
Q

facilitates O2 diffusion to the mitochondrion

A

Mb

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3
Q

function of Mb

A

intracellular transport and temporary storage of O2 needed for aerobic metabolism of muscle

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4
Q

secondary structure of Mb

A

8 a-helices

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5
Q

quaternary structure of Hb

A

a2B2

  • 2 x a:B dimers
  • quilibrium favors tetramer
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6
Q

ApoHb vs HoloHb

A

protein without vs with prosthetic group

-HoloHb = 1 heme/subunit = 4 hemes

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7
Q

how many hemes/O2 binding sites in Hb

A

4 (1/subunit)

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8
Q

basis for Hb’s cooperative binding, resulting in a sigmoid binding curve

A

T vs R

-R = more O2 bound = higher O2 affinity until Hb molecule is sat’d

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9
Q

porphyrin

A
  • tetrapyrrole

- forms protoporphyrin IX, which chelates Fe

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10
Q

metal chelating site on Hb

A
  • binds Fe

- 4 nitrogens of 4 pyrrole groups point inward

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11
Q

substituent groups on heme prosthetic group (a pyrrole)

A

4 methyl, 2 vinyl, 2 propionate

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12
Q

state of Fe in deoxyHb

A

ferrous = Fe(II)

-reduced

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13
Q

(high/low) O2 affinity at P50

A

high

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14
Q

Mb vs Hb curve

A

hyperbolic vs sigmoidal

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15
Q

Mb ___ O2 in conditions under which Hb ____ it

A

binds

releases

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16
Q

Which has higher P50 (Mb/Hb)

A

Hb

17
Q

O2 binding negative effectors

A

decrease affinity of O2 for Hb allows unloading in tissues, while loading can occur in lungs
-BPG, CO2, H+

18
Q

O2 binding positive effectors

A

increase affinity of O2 for Hb - bad, can’t unload

19
Q

BPG

A

stabilizes T state, lowers affinity of Hb for O2

20
Q

BPG binds to and stabilizes ______, and ______ Hb’s affinity for O2

A

T quarternary state of Hb

decreases

21
Q

Hb’s affinity for O2 is fine-tuned by altering this concentration in the blood

A

BPG

22
Q

shift Hb curve right

A

unload

ex. BPG

23
Q

short term acclimation to low O2 pressure

A

shift Hb curve right with BPG; deliver same amt of O2 as at sea level without reducing tissue O2 pressure

24
Q

does pH modulate Mb’s affinity for O2?

A

no

25
Q

pH in lungs which allows for higher Hb-O2 affinity

A

high pH, low [H+]

26
Q

pH in tissues which allows for lower Hb-O2 affinity

A

low pH, high [H+]

27
Q

carbamylation of Hb

A
  • CO2 combines reversibly with N on protein

- favors T state - reduced Hb-O2 affinity

28
Q

effect of CO2 and H+ on HB-O2 affinity

A

capillaries: CO2 stabilizes T state, O2 is released

- H+ further reduces affinity

29
Q

why does fetal Hb bind O2 with higher affinity

A

fetal Hb has lower affinity for BPG

30
Q

HbS

A
  • a2B2

- sickle cell anemia

31
Q

HbH

A
  • B4

- a-thalassemia

32
Q

HbBarts

A

gamma4

-a-thalassemia

33
Q

methemoglobin

A

ferric - doesn’t bind O2

34
Q

sign of methemoglobinemia

A

cyanosis