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21 fall: Biochem > Test 2 Lecture 32-33 > Flashcards

Test 2 Lecture 32-33 Flashcards

1
Q

___ is the O2 carrier protein of the blood.

A

hemoglobin

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2
Q

___ is an O2 storage protein found in muscle

A

myoglobin

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3
Q

Hemoglobin has a _______ affinity for O2 in the lungs, which promotes O2 uptake and has a ____ affinity for O2 in the tissues, which promotes the release of O2.

A

high

lower

“protein intelligence”

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4
Q

Hemoglobin assists in the transport of CO2 from ___ to the ___

A

tissues

lung

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5
Q

High concentrations of ___ provide an O2 reserve in the muscles of diving birds and mammals.

A

myoglobin

store O2 in muscles, don’t need to breathe when diving

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6
Q

Myoglobin is composed of ___ helixes

A

aplha

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7
Q

The heme of myoglobin is bound ___

A

tightly but not covalently, can come off under extreme conditions

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8
Q

Heme is attached to myoglobin by ___ and ___

A

proximal histidine

distal histidine

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9
Q

The proximal histidine of myoglobin attaches to the ___

the distal histidine ___

A

iron of the heme

hovers above where O2 will bind, Water sits in that places when waiting for O2

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10
Q

iron in hemoglobin is in the ___ state

A

+2

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11
Q

when O2 is not bound to iron of hemoglobin the iron is ___

when O2 is bound to the iron of hemoglobin the iron is ___

A

big and pulled down by the proximal histidine

now in +3 state, gets smaller and is pulled in line with the heme

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12
Q

when O2 binds to iron of heme, Iron changes from ___ to ___ and the O2 forms a ___

A

+2

+3

superoxide ion

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13
Q

Distal histidine is H-bonded to bound oxygen with the H-bonding to the ____form being tighter.

A

superoxide

distal histidine binds better when Iron 3+

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14
Q

Distal histidine binding to the superoxide form inhibits the release of superoxide ions and the _____ of the iron

A

oxidation

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15
Q

Oxidized hemoglobin with Fe3+ is called ____ and does not bind O2.

A

methemoglobin

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16
Q

___ uses NADH to reduce methemoglobin and reform hemoglobin.

A

Methemoglobin reductase

high levels of methemoglobin leads to comma, seizures and death

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17
Q

In cats and dogs an intermediate of acetaminophen(tylenol) metabolism leads to formation of _________. Cats are very sensitive to this effect. Acetaminophen can also cause liver damage.

A

methemoglobin

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18
Q

Leads to the formation of methemoglobin in dogs, cats, and other animals. Clinically significant levels of methemoglobin have occurred.

A

Benzocaine

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19
Q

Seen in ruminants eating nitrate-accumulating plants, especially plants treated with nitrogen containing fertilizers. Nitrate is reduced to ______ by ruminal microbes

A

nitrite (cause the formation of methemoglobin)

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20
Q

why is methemoglobin bad

A

Iron in +3 state, can not bind with O2, Oxygen can not be carried to tissues

“internal suffocation”

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21
Q

Onion toxicity and Heinz bodies

A

Has been seen in cattle, sheep, horses, dogs and cats.

Onion and other plants contain chemicals that can oxidize cysteine residues in hemoglobin to disulfides, ultimately leading to denaturation and aggregation of hemoglobin. Aggregates of denatured hemoglobin in the red blood cells are called heinz bodies. Half-life of affected red blood cells is reduced. Cats are very sensitive to formation of Heinz bodies.

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22
Q

Aggregates of denatured hemoglobin in the red blood cells are called _________

A

heinz bodies

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23
Q

Half-life of affected red blood (Heinz bodies) cells is ____. ____ are very sensitive to formation of Heinz bodies.

A

reduced

Cats

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24
Q

This enzyme reduces methemoglobin back to hemoglobin

A

Methemoglobin reductase

a.k.a. cytochrome b5 reductase

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25
Methemoglobin reductase deficiency symptoms
lethargic and exercise intolerant, but typically live normal length lives.
26
explain how distal histidine reduces the affinity of carbon monoxide for Iron
Carbon monoxide likes to bind perpendicular to heme distal histidine forces it to bend= unhappy CO O2 likes to be bent, will happily sit there
27
Distal histidine forces Carbon monoxide to bind in a ________ conformation. This ______ the affinity of CO for hemoglobin/myoglobin, without decreasing the affinity of hemoglobin/myoglobin for \_\_\_\_\_, which naturally binds in a bent conformation.
bent lowers oxygen
28
Hemoglobin/myoglobin still bind to carbon monoxide ____ times more tightly than oxygen, which means that CO can block the binding of O2 to hemoglobin and interfere with O2 transport.
120 to 500
29
treatment for CO
long term oxygen therapy hyperbolic chamber
30
What other heme-containing protein complex is a target in CO poisoning?
cytochrome c oxidase final part of the electron transport chain
31
what is this showing
myoglobin
32
Myoglobin is a monomer that binds O 2 at a ___ high affinity site.
single
33
Is myoglobin a good protein for transporting O2? Why or why not?
no binds too well, does not want to let O2 go binds really fast, really well in low amounts of O2
34
Hemoglobin is a ___ . Made of \_\_\_\_
tetramer 2 alpha and 2 Beta subunits O2 binding changes the conformation of hemoglobin and its affinity for oxygen
35
\_\_\_ binding changes the conformation of hemoglobin and its affinity for oxygen
O2 when O2 binds, the whole hemoglobin changes shape, to allow more O2 to bind
36
hemoglobin can bind to ___ O2 but they like to live in either ___ or \_\_\_\_
4 no oxygen 4 oxygen
37
if Hemoglobin has 3 O2 it is more likely to ___ an oxygen, then a hemoglobin with 1 O2, which will \_\_\_an oxygen
get/take give away
38
concerted model of positive cooperatively is also called the
matthew effect Hemoglobin in R state like to take O2 want to have 4 Hemoglobin in T state, like to give away O2 want to have 0 oxygen
39
Hemoglobin in ___ state like to take O2 want to have 4 Hemoglobin in \_\_\_state, like to give away O2 want to have 0 oxygen
R T
40
Matthew effect leads to
most hemoglobin is either **fully oxygenated** (4 O2) **completely deoxygenated** (no O2) rare intermediate oxygenated forms
41
explain
Myoglobin: binds very fast and completely at low O2 Hemoglobin takes time: at first has low affinity for O2, will bind slow (T state) but as it gets more O2, affinity for O2 will increase, will bind faster (R state), will reach full saturation in the lungs around 100 torr
42
**when at rest**: 21% of oxygen available in hemoglobin has been given away (normal steady state activity **When exercising:** 66% of oxygen has been used. This is on steep part of curve, want to have more O2 delivered when needed, can drop to very low amounts of O2
43
bohr effect
(lower pH) Protons and CO2 preferentially bind to the low affinity T-state of hemoglobin and increase the release of O2 lower pH (lactic acid)(protons) and CO2 will stabilize the T state and will promote the release of O2 form hemoglobin At lower pH, there is a higher concentration of protons, there protons will bind to R state Hemoglobin and turn it into T state Hemoglobin and 4O2
44
bohr effect At lower pH, there is a **higher concentration of protons**, there protons will bind to R state Hemoglobin(full Heme) and turn it into T state Hemoglobin and 4O2
45
The affinity of ionizable groups for protons can be altered by their \_\_\_
microenvironment pKa
46
When the pH = pKa the protonated and unprotonated forms are present in ___ amounts.
equal
47
When pH is below pKa, ___ form is favored, When pH is above pKa, ___ form is favored.
protonated unprotonated
48
At physiological pH, ~ pH 7.4, an unperturbed histidine will be mostly \_\_\_\_\_\_\_
unprotinated pH 7.4 is higher then pKa 6.5 therefore histidine will live in unprotinated form
49
In the T-state, histidine 146 is in close proximity to aspartate 94. This greatly ________ the protonation of this histidine residue.
increases
50
Lower blood pH will __ the protonation of histidine 146 and other groups that stabilize the T-state and increase the release of oxygen from hemoglobin.
increase
51
explain
at lower pH: blue curve: Bohr effect lower pH will trigger T state hemoglobin, Hemoglobin will want to give away its O2 therefore at 20 torr in exercising tissues, hemoglobin will give away 77% of O2 instead of 66% at normal pH **lower pH= more acid= more need for O2**
52
The binding of CO 2 to hemoglobin stabilizes the \_\_
T state Carbamate is negative charge, will stabilize T state (give away O2, graph moves to the right)
53
how does Carbon dioxide promote the Bohr effect
CO2 + H2O→ carbonic acid → bicarbonate- and H+ CO2 changes into an acid, which will lower pH and increase Bohr Effect, stabilize T state more Oxygen will be released
54
red: normal hemoglobin (give away 66% of O2 blue: low pH and no CO2 (give away 77% O2) purple: lower pH and CO2 (give away 88% O2) increase CO2= more acid= decreased pH **right = more T state= more O2 given away**
55
In the tissues, hemoglobin in the T-state increases the CO2 carrying capacity of the blood by directly binding CO2, and by binding protons, which increases the amount of bicarbonate in the blood by ____ blood pH.
increasing hemoglobin acts as buffer
56
In the lungs, the high concentration of O2 drives hemoglobin to the\_\_\_.
R state | (wants to bind to O2, wants 4 of them)
57
In the lungs, the high concentration of O2 drives hemoglobin to the R-state. This leads to a release of ____ and ___ from hemoglobin, which _____ blood pH and increase the release of CO2 from the lungs.
protons CO2 decrease
58
In the lungs, the high concentration of O2 drives hemoglobin to the R state. These effects roughly _______ the efficiency of CO2 transport from tissues to lungs
double
59
Hemoglobin is the most important protein ___ of the blood.
buffer increase pH, make less acidic, binds to H+(protons)
60
2,3-Bisphosphoglycerate Decreases the Affinity of Hemoglobin for ____ in Some Species
oxygen triggers hemoglobin to let go of O2 (shifts towards T state- to the right)
61
2,3 BPG is made from \_\_\_\_
1,3 diphosphoglyerate. intermediate from glycolysis RBC go through glycolysis for energy: this intermediate is used by hemoglobin to promote release of O2
62
2,3 BPG only binds hemoglobin in the ______ This shifts the hemoglobin O 2 binding curve to the \_\_\_
T state right
63
why can't BPG bind to R state
no room in the R state
64
The BPG effect is not seen in all animals. It is present in most ____ .
primates, marsupials, horses, camels, dogs, pigs and rodents
65
In birds a similar role to BPG is served by \_\_\_\_.
inositol pentaphosphate
66
No BPG effect is seen in cattle, sheep, goats, deer, cats and lemurs; in these animals hemoglobin has an inherently lower affinity for \_\_\_
oxygen, hemoglobin doesn't bind as well, therefore doesn't need BPG to let go of Oxygen
67
In some animals BPG can be used to fine tune hemoglobin saturation curve by
**change BPG can change how hemoglobin binds to O2** BPG increases in high altitudes curve to the right (toward T state) (lets go of O2) More O2 delivered to tissues
68
red: fetal blood, has higher affinity for O2, shifts to the R state low BPG, wants to hold O2 more
69
Mechanism is species specific. In some species, fetal hemoglobin binds BPG with a _____ affinity, which shifts the O2 binding curve to the left.
lower In dogs, horses and pigs, fetal red blood cells have much lower concentration of BPG. In ruminants, fetal hemoglobin has an inherently higher affinity for O2 than adult hemoglobin.
70
why do we need artificial blood
blood not always available blood can have diseases blood can have immune reaction blood goes bad
71
issues with using free hemoglobin as O2 carriers
free hemoglobin is rapidly removed from the blood, tetramer will break apart No 2,3 BPG- this is needed for proper O2 curve
72
Oxyglobin
glutaraldehyde crosslinked bovine hemoglobin
73
5 reasons glutaraldehyde crosslinked bovine hemoglobin is good
1. Highly purified hemoglobin- no immune reaction compatibility issues 2. Crosslinking stabilizes hemoglobin tetramer (will not break apart) 3. Bovine hemoglobin **does not use 2,3 BPG**, so its O2 binding curve is unaffected by the absence of BPG. 4. Not highly antigenic 5. Causes vasoconstriction (good or bad)
74
Nitric oxide (radical) is produced by endothelial cells from arginine by an enzyme called \_\_\_
nitric oxide synthase
75
Nitric oxide is short-lived (few seconds) and in the blood vessel produces local \_\_\_\_.
vasodilation.
76
\_\_\_\_ binds Nitric oxide and inhibits nitric oxide signaling
free hemoglobin inhibits nitric oxide, will cause vasoconstriction nitric oxide can't get into red blood cells therefore doesn't bind to hemoglobin in RBC
77
Nitric oxide is involved in many other processes including \_\_\_\_
immune defense uses Nitric oxide as free radical to kill invading organisms
78
Nitric Oxide activates ___ synthesis; in immune defense it can function as a reactive free radical as well as a signaling molecule
cGMP
79
What drugs work on nitric oxide pathway
viagra (breaks down cGMP, acts as vasodialtor) nitroglycerin

21 fall: Biochem (44 decks)

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