Lecture 23 Oxidative Phosphorylation Flashcards

(37 cards)

1
Q

in the ETC where are you pumping protons to?

A

you are pumping protons from the matrix into the intermembrane space

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2
Q

why are there so many folds of the intermembrane?

A

to maximize surface area to do the most ETC and ATP synthase as possibe

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3
Q

Is e- transport requires for ATP synthesis?

A

no, if you maintain proton gradient, then your good.

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4
Q

What is valinomycin?

A

an ionophore that can carry K+ through the membrane down its chemical gradient

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5
Q

what does complex 5 do? in terms of proton gradient

A

uses the proton gradient produced by the ETC to move proteins down its concentration gradient from the intermembrane space back into the matrix to make ATP

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6
Q

What is the “N” side of the membrane?

A

the matrix, which is the negative of the membrane

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7
Q

What is the “P” side of the membrane?

A

the intermembrane space, which is Positive (bc you pumped all those protons over there)

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8
Q

What is another name for atp synthase that’s not complex 5?

A

FoF1 ATPase
Fo (membrane soluble part) part refers to the potion of the complex that is inside of the membrane and
F1 refers to the (peripheral) part of the complex that is hanging out of the matrix side (F1 potion is dissociable and you can seperate the integral and peripheral portions)

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9
Q

Peripheral part of ATPase

A

F1

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10
Q

Integral part of ATPase

A

Fo

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11
Q

which part of ATPase is responsible for dragging protons across the membrane?

A

F0

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12
Q

What direction is ATP synthase rotation if its doing ATP hydrolysis?

A

Counter clockwise

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13
Q

What direction is ATP synthase rotation if its synthesizing ATP?

A

Clockwise

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14
Q

Does ATP synthase rotate differently depending on if its synthesizing of hydrolyzing ATP

A

yas queen I would just be doing the reverse reaction so it would just move backwards

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15
Q

Why and how does Fo Rotate?

A

because you have a continuous sexy proton gradient each H+ that moves into F0 is met with an aspartic acid that get protonated by the H+, and as more H+ come, the deprotonated aspartic acids grab the protons causing the protonated apratice acids to move out of the way and rotate counter clockwise (this is talking about if you’re doing synthesis of course) kind of like a revolving door rat race situation

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16
Q

Why is the F₀ portion of ATP synthase named “F₀”

A

named for its sensitivity to Oligomycin, an antibiotic that specifically stops ATP synthase by binding to the Fo which “puts a wrench in the revolving door” and keeps it from moving protons

17
Q

how many diffrent Alpha and beta dimers are there in the F1 portion of the ATPase

A

3, like a 6 petal flower

18
Q

Oligomycin

A

an antibiotic that binds to Fo part of ATPase and stops its form rotating and therefore stops it all together

19
Q

how many protons are needed for each synthesis of ATP

20
Q

does F1 act like a MM enzyme

A

No! bc the off rate (letting go of the fully formed ATP) is actually the rate limiting step (the slowest)

21
Q

what makes the alpha and beta subunits change conformation to either favor binding, catalysis or release ATP

A

the rotation of the gamma, epsilon and C (F0) portion of the synthase by the introduction of protons

22
Q

What is the ΔG (Gibbs free energy change) of moving a proton through ATP synthase (ATPase)

A

around -20 kj/mol

23
Q

Does shutting off the ETC shut off ATP ase

24
Q

what do ETC uncouplers? examples? what characteristics do uncouplers have to have?

A

They uncomple the ETC and rip protons shutting off ATPase
-they can freely diffuse across membrane and carry H+ (they are a type of ionophore)
-they have to be hydrophobic
-they can be protonated

25
What is DNP
A type of uncoupler (the diet thing)
26
Why do you require ADP to start the ETC reduction of water?
Just because you need the ingredients to make ATP synthase to go and if you cant make ATP synthase go then you lock the whole ETC in place
27
What is the uncompler that helps animals hibernate
Thermogenin (an uncoupling protein)
28
What does the C complex do in ATPase
pumps protons and rotates
28
technically 3 protons are needed to make an ATP, why do you need the 4th?
To move the inorganic Phosphate into the intermembrane space
29
Where does glycolysis happen?
in the cytoplasm
30
Why do you need an NADH shuttle?
bc there is lots of NADH in cytoplasm that cant be used for ETC unless you get it into the matrix
31
Pathway NADH of muscle and brain Dihydroxyacetone phosphate G3P shuttle
1. cytoplasm- using NADH reduce DHAP to G3P which is able to permeate the outer membrane 2. intermembrane space- oxidize G3P back into DHAP (where it goes on its merry way) using G3P dehydrogenase that reduces FADH2 so that its in the inner membrane and able to directly go into complex 3 as that FADH2
32
what part of the body does the NADH Dihydroxyacetone phosphate. G3P shuttle happen
Muscles and brain
33
what energy consequence does the NADH Dihydroxyacetone phosphate G3P shuttle and why is it okay
reduces overall net ATP by 2 because you're going into ETC as FADH2 instads of NADH but its chill bc your brain and muscles need so much energy it will take the hit
34
What part of the body does the Malate- Aspartate shuttle happen in, and is there an energy consequence?
liver, heart, kidney, NO
35
Steps in the malate- aspartate shuttle
1. (in intermembrane space) Reduce oxaloacetate using NADH and turn it into Malate 2. the malate has a transporter for itself (she's special) 3. once in the matrix you just oxidize that maleate to get your NADH out back into oxaloacetate 4. But how do you get you oxaloacetate back out???(there are no shuttle for her) 5. you do a side reaction that turns that ho into an aspartate (by aminotransferase IE transamination using glutamate and alpha ketoglutarate) where its then able go through a transporter and then tranaminate it again once its in the IM space back to oxaloacetate where its able to shuttle again!!!!
36
which is more efficent DHAP or aspartate malate
DHAP is faster but has -2 aura aspartate malate is slower but nothing is lost