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Mitochondrial > Lecture 4 > Flashcards

Lecture 4 Flashcards

1
Q

Another name for ATP synthase

A

Complex V

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2
Q

What is ATP synthase responsible for

A

Generating ATP

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3
Q

You produce the same amount of ATP as ____ in a single day

A

Your weight

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4
Q

How is F0F1 ATPase portrayed

A

Globular protein with a transmembrane region

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5
Q

What is ATP produced from

A

ADP and inorganic phosphate

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6
Q

Major regions of ATPase

A

F0 and F1

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7
Q

How many subunits in F1

A

5

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8
Q

How many subunits in F0

A

3

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9
Q

___ is similar in size to the F1 region

A

Complex I

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10
Q

Is F0F1 ATPase the only type of ATPase

A

No

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11
Q

Other types of F0F1 ATPase

A

E1E2 ATPase and V ATPase

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12
Q

Type of E1E2 ATPase

A

Na+/K+ pump

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13
Q

Type of V ATPase

A

Vacuole H+ pump

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14
Q

Function of Na+/K+ pump

A

Work under ATP hydrolysis (break it and harness the energy to perform useful work)

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15
Q

Function of V ATPase

A

Pump protons

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16
Q

Where is V ATPase located

A

Vacuole

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17
Q

ATPases are energy-dependent ____

A

Ion pumps

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18
Q

ATPases have reversible function depending on ___

A

The environment

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19
Q

Similar features that all ATPases share

A
  • Ability to reverse

- Series of shared structures

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20
Q

Shared structures that ATPases have

A

F1 analog and F0 analog

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21
Q

The overall function of ATPase is to throw the equilibrium between ___ and ___ out of balance

A

ATP and ADP

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22
Q

Proportion of products versus reactants

A

Mass action ratio

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23
Q

Use ___ to maintain mass action ratio away from equilibrium

A

Delta P

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24
Q

ATPase sustains ____

A

Mass action ratio

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25
Q

ATPase sustains the mass action ratio __-__ orders of magnitude away from equilibrium

A

7-10

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26
Q

What does sustaining the mass action ratio lead to

A

Thermodynamic favoring reaction

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27
Q

What do thermodynamic favoring reactions produce

A

ATP

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28
Q

What was studied to examine ATPase

A

Submitochondrial particles (SMPs)

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29
Q

What are SMPs

A

Reconstituted membrane regions of the mitochondria that allow researchers to evaluate the functions of proteins

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30
Q

Most SMP have ___ structure

A

Inverted membrane structure

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31
Q

Inverted membrane structure

A

Matrix facing outside and inner portion represents cytoplasmic side

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32
Q

What is the benefit of inverted membrane structure

A

Further manipulation of proteins

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33
Q

In the inverted membrane structure, F1 faces the ___

A

Matrix

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34
Q

Where is ATP generated and hydrolyzed

A

Matrix

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35
Q

What did early studies treat SMP with

A

Urea and kealating agents

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36
Q

What is the effect of urea treatment on SMP

A

Some F1 regions knobs were lost

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37
Q

What happens when F1 knobs are lost

A

SMPs cannot synthesize ATP without them

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38
Q

How did F1 get its name

A

First fraction (F1). Called the first fraction because it was the first lost

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39
Q

Can protons still be channeled through the membrane when F1 is lost

A

Yes

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40
Q

What are membrane channels inhibited by

A

Oligomycin

41
Q

What does oligomycin manipulate

A

F0

42
Q

How did F0 get its name

A

Stands for oligomycin fraction

43
Q

F1 subunits kDa

A

370

44
Q

F1 subunits

A

alpha 3, beta 3, gamma, epsilon, sigma

45
Q

F0 subunits kDa

A

160

46
Q

F0 subunits

A

Transmembrane alpha helices; 9-12 c subunits, 2b, and 1 a subunits

47
Q

___ and __ subunits interact, transferring rotation from F0 to F1

A

C and gamma

48
Q

Gamma is the rotor that connects __ and __

A

F1 and F0

49
Q

What is the C ring composed of

A

Alpha helices

50
Q

What happens to the C ring as protons are translocated from intermembrane space into a and c subunits and then matrix

A

C ring rotates

51
Q

After rotation of the C ring, there is a transfer of torq through the ___ subunit

A

Gamma

52
Q

What does the transfer of torq cause

A

Gamma to rotate on its axis

53
Q

Rotation of gamma triggers changes in the shape of ____

A

Alpha and beta subunits

54
Q

How many subunits in the C ring

A

About 10, estimated 9-12

55
Q

Inhibitor protein can interact with ___ and inhibit ____

A

Beta subunits

Formation of ATP

56
Q

Why is inhibitor protein present under natural conditions

A

So reaction does not run backwards (controls reversible function of ATPase)

57
Q

How to reverse a reaction

A

Change the abundance of products versus reactants (MAR)

58
Q

What does it mean when a ATP synthase reaction is reversed

A

Turn ATP synthases into an ATP hydrolyzing machine

59
Q

___ allows the gamma subunit to rotate as ATP is hydrolyzed

A

Anchored F1

60
Q

How to record gamma subunit rotation

A
  • Remove F1 region and manipulate it to attach actin filament to gamma subunit
  • Actin filament contains a fluorophore
  • Record movement of actin filament under given conditions
  • Tag F1 subunit with histidine group to attach it to a cover slip
61
Q

How many revolutions of gamma per second

A

130

62
Q

What subunits are active sites for ATP synthesis

A

3 beta subunits

63
Q

___ ATP hydrolyzed per second

A

390

64
Q

Where does catalytic formation occur

A

beta subunit

65
Q

F0 rotates as a product of ___

A

H+ translocation

66
Q

Gamma subunit is twisted by ___

A

F0

67
Q

Rotational force of gamma subunit translates to conformational changes in _____

A

a and b subunits

68
Q

Where does catalytic formation occur

A

3

69
Q

Is the gamma subunit center

A

Usually a little off center

70
Q

Changing shape of alpha and beta subunits leads to ___

A

Interaction of subunits with ADP and inorganic phosphate

71
Q

How many times does the rotation cycle complete

A

3

72
Q

ATP stores energy in the form of ____

A

High energy phosphate group

73
Q

Composition of ATP

A

Adenosine ring with a chain of 3 phosphate groups attached

74
Q

How is energy released from ATP

A

The last phosphates can be split off to release the energy within the bond

75
Q

What are the resulting products of breaking of ATP

A

ADP and inorganic phosphate

76
Q

Mitochondria make ___ kg of ATP a day in an adult

A

60

77
Q

How many motors are in ATP synthase

A

2

78
Q

Motors of ATP synthase

A

F1 and F0

79
Q

Where is F0 located

A

Within the membrane

80
Q

Where is F1 located

A

At the top

81
Q

F0 is __ powered

A

Proton

82
Q

What is proton flow driven by

A

pmf

83
Q

How is F0 proton powered

A

Protons flow through a channel open to just the intermembrane space where they bind to a ring of protein subunits, rotate 360 degrees, and exit through another channel exposed only to the matrix

84
Q

Torq is generated by ___ and transferred to __ by ____

A

F0
F1
Central stalk

85
Q

___ is responsible for generating ATP by adding phosphate to ADP

A

F1

86
Q

Conformation changes of catalytic subunits caused by

A

Rotation

87
Q

Catalysis occurs at the interface between ___

A

Dimers

88
Q

Three distinct states of ATP synthesis

A
  1. ADP and phosphate bind to the catalytic site, and the central staff rotates 120 degrees to rearrange the molecules
  2. Enzyme undergoes a further 120 degree rotation, and ADP and P are fused together to produce ATP
  3. Enzyme rotates again to return to starting position, where ADP is released, and ADP and P can be bound for the next cycle
89
Q

Catalytic subunits must remain stationary with respect to ____

A

Rotating central shaft

90
Q

How are catalytic subunits kept stationary

A

Scaffold on the outside of the complex (peripheral stalk)

91
Q

Is the peripheral stalk dynamic

A

Yes (can accommodate)

92
Q

What does ATP synthase dimerize to shape the mitochondrial inner membrane into

A

Signature cristae shape

93
Q

Purpose of signature cristae shape

A

Turbo charges ATP synthase by focusing proton gradient near ATP synthase

94
Q

Complexes are in very close proximity to ____

A

ATP synthase

95
Q

Can ATP synthase interact with each other

A

Yes, they can dimerize

96
Q

Where is ATP synthase highly concentrated

A

In regions where ETS complexes are most abundant

97
Q

Why is ATP synthase highly concentrated in regions where ETS complexes are most abundant

A

Helps to take advantage of electrochemical and proton gradient

98
Q

What membrane does the lipid mosaic model apply to

A

Inner membrane

Mitochondrial (5 decks)

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