Chem final Flashcards

1
Q

What is the diff between myoglobin and hemoglobin

A
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2
Q

Structurally, what are the similarities between Hb and myoglobin

A

Both are composed of a heme complex that have a coordinated Fe ….

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3
Q

T/F: Heme on its own is soluble

A

False

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4
Q

What ligands can attach to heme? (4)

A
  1. oxygen
  2. CO
  3. CO2
  4. Cyanide (cytochromes)
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5
Q

In regards to oxygen binding, what is the diff between myoglobin and Hb?

A
  1. Myoglobin has a higher affinity to oxygen, is monomeric, non cooperative binding
  2. Hemoglobin is tetrametric (4 domains), cooperative binding,
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6
Q

A rightward shift on an association curve for oxygen binding means?

A

less affinity for oxygen

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7
Q

When does myoglobin release oxygen?

A

When levels in muscles are very low

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8
Q

T/F: Hemoglobin can bind to oxygen multiple times

A

true

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9
Q

The sigmoidal shape of the hemoglobin curve signifies

A

cooperative binding

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10
Q

When does oxygen affinity increase for Hb?

A

as more oxygen is bound to heme (saturation increases)

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11
Q

Why do we see an increase in oxygen binding affinity with hemoglogin?

A

As oxygen binds, there is a shift in the heme and shift in protein structure
(Tense “t” state to Relaxed “r” state)

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12
Q

Binding always leads to ________ and with Hb this causes more _______

A

confirmational change
oxygen affinity

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13
Q

What is the R state?

A

4 oxygen have bound to Heme

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14
Q

what is the diff between fetal Hb and adult Hb

A

fetal has a higher affinity for oxygen

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15
Q

Why is there a higher affinity for oxygen in fetal Hb?

A
  1. Structural differences ( adult have 2 alpha and 2 beta)
  2. 2,3 BPG
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16
Q

Does 2,3 BPG bind to fetal Hg?

17
Q

Why does 2,3 BPG do to adult Hb?

A

preturbe oxygen from binding to Heme

18
Q

What charge is on histadine rings in adult Hb?

19
Q

What charge is on serine residue in fetal Hb?

20
Q

Why is there no ion-dipole intermolecular force between 2,3 BPG and fetal hemoglobin

A

The distance is too great because the serine is small

21
Q

2,3 BPG which stabalizes the structure of Hb, can also be a

A

competitive inhibitor

22
Q

Shifting equilibrium to the left means? Would 2,3 BPG binding to adult Hb cause this?

A

higher affinity for oxygen
no; there would be a shift to the right

23
Q

Where does 2,3 BPG come from

A

our bodies produce it

24
Q

What does 2,3 BPG essentially do?

A

prevent conformational change and disallow more oxygen from binding

25
T/F: Both adult and fetal hemoglobin curves are sigmoidal
true
26
Shifting equillibrium to the left means oxygen favors the
T state
27
how can heme overcome binding of 2,3 BPG?
increasing pressure of O2
28
What are the 3 ways Co2 is transported throughout the blood? Which is primary?
1. dissolved gas (10%) 2. bicarb (blood buffering system)* 3. bound to protein of the Hb
29
The n terminus of an amino acid is ________ while C is ________
nucleophilic electrophilic
30
CO2 bound to Hb is called?
Carbaminohemoglobin
31
Where does CO2 bind on Hb?
the apoprotein, not the heme
32
High affinity for CO2 causes a _______ affinity for O2
low
33
What happens when RBC starts to bind to CO2
localized changes in pH of the environment (Bohr-Haldane Effect)
34
Oxygen dissociation is increased by (3)
1. Increasing temp 2. Lowering blood pH 3. increasing partial Pco2
35
What affects does increasing Pco2 have in the blood? (3)
1. Increase H concentration 2. protonates certain amino acid residues 3. leads to conformational change of protein
36
CO binds _____ times more strongly to heme than O2
200-300
37
T/F: CO2 binds to the same site as oxygen and CO does not
False CO binds to the same site as O2 on heme and CO2 does not CO2 prevents conformational change
38
Is binding reversible once CO bound to heme? how?
yes; increase the O2 levels or pressure
39
When does fetal Hb dissipate in children and convert to adult Hb?
around 6 months