ATP synthase Flashcards

1
Q

Who proposed the chemiosmotic model?

A

Mitchell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What did the chemiosmotic model proposed?

A

PMF conserves energy of electron transfer and drives ATP synthesis as protons flow back into mm via proton pore Fo in inner mm.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is needed to produce ATP?

A

ADP, Pi and succinate.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are the 2 coupled reactions of ATP synthesis?

A

ATP synthesis and O2 production.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What blocks the electron transport and stops O2 consumption and ATP synthesis?

A

Cyanide.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What reagents mimic proton influx/efflux?

A

DNP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What did the chemiosmotic model show?

A

That e-transfer, OMF and ATP synthesis are obligately coupled.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What do inhibitors of the electron transport block?

A

ATP synthesis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What do inhibitors of ATP synthesis block?

A

Electron transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Which scientist worked out how PMF causes enzyme ATP synthase to synthesise ATP?

A

Walker

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What do the ATP synthase complexes in the mitochondria make?

A

The ATP required to sustain life by a rotary mechanism.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

ATP synthase enzyme is what type of enzyme and how many distinct functional domains does it have?

A

F-type ATPase purificed and crystallised has 2 distinct functional domains F1 and F0

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is human ATP synthase assembled from?

A

27 nuclear encoded genes and two mitcondrondrially encoded genes.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What type of protein is F1?

A

It is a peripheral membrane protein - is hydrophilic.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Which side is the F1 protein on ?

A

The N side - negative side, it is attached to inner mitochondrial membrane.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Which protein F1 or F2 is the catalytic domain - where ATP is synthesised.

A

F1

17
Q

What type of protein is F0?

A

It is an integral membrane protein - hydrophobic.

Spans the mitochondrial inner membrane proton pore?

18
Q

In F0, what takes place?

A

The H+ move through it against conc gradient from intermembrane space through F1 to matrix - this proton flow enables ATP synthesis.

19
Q

Describe the F1 structure?

A

9 subunits - 5 different types.
A3, B3, y, delta, epsilon
A and B alternate around the central y shaft.
A and B have binding sites

20
Q

Which are the more important subunits in the F1 structure?

A

The Beta subunits - can bind ADP, ATP or be empty

21
Q

Which protein makes up the proton pore?

A

The integral F0 protein.

22
Q

Which subunits is F0 composed of?

A

ab2cn

23
Q

Which is the more important subunits in F0?

A

C subunits - clindar like structure with pore number of C subunits difference b/w species 8-15

24
Q

What do the C subunits in F0 do?

A

They rotate together around a perpendicular axis - around epsilon and gamma which ‘stand’ on C subunits.

25
Q

Which protein was purified first?

A

F1 - could only synthesis ATP when F0 was added.

26
Q

What components are needed for ATP synthase to work?

A

F0 - bind ATP and ADP + Pi = synthesise ATP

F1 = ATP bound tightly and that proton energy needed to ‘dislodge’ it.

27
Q

Which direction does proton energy flow through?

A

F0 to F1

28
Q

What did Boyer propose?

A

That the binding change mechanism to explain how ATP synthase synthesises ATP.

29
Q

What causes the F1 to rotate?

A

When protons pass through F0 and cause cylinder of c units attacked to gamme (subunit of F1 to rotate about long axis of gamma)

30
Q

Which subunits rotates?

A

The y subunits and passes through the centre of alpha 3 and beta 3 which are stationary

31
Q

Which catalysis causes ATP synthesis?

A

Rotational

32
Q

Which subunits are the ATP and ADP bound to?Which is more tightly bound?

A

Beta subunits, ATP is more tightly bound

ADP also has Pi

33
Q

Which subunit rotates and comes into contact with each beta subunit in succession?

A

gamma

34
Q

How many protons induce a rotation and what is the degree of rotation? How many ATP are formed?

A

3 protons induce a rotation of 120 degrees. 1 ATP formed

35
Q

How many conformations and ATPs are syntehsised in a full rotation?

A

360 degree = beta gone through 3 conformations and 3 ATP synthesised.

36
Q

Can the ATP synthase work in reverse?

A

Yes, in ATPase breaking down.

37
Q

Which type of microscopy enabled visualisation of the gamma subunit rotating due to proton flux through F0 cylinder of C subunits.

A

Atomic Force Microscopy

38
Q

How is OXPHOS regulated?

A

Regulation of enzymes in glycolysis, fat catabolism, citric acid cycle and OXPHOS integrated to maintain constant ratio of ATP/ADP(Pi)

39
Q

What affects the regulation og OXPHOS?

A

The energy needs of the cell/tissue & organism.

Can become impaired in aging