Mechanism of ATP Synthesis Flashcards

1
Q

What regulates passage of H+ through the FO membrane?

A

F1

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2
Q

Which ATP synthase domain faces the matrix?

A

F1 ATPase

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3
Q

What is the structure of F1FO ATPase?

A
  • 3 alpha and 3 beta subunits
  • Connected centrally by a gamma, sigma, epsilon subunit
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4
Q

How can F1 and FO be separated?

A

By treatment with low salt/urea

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5
Q

When F1 is separated does it have ATPase activity?

A

Yes

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6
Q

When F1 is separated does it have ATP synthesis activity?

A

No

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7
Q

In FO what does the addition of oligomycin do?

A

Inhibits H+ permeability

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8
Q

When FO is separated what happens to its activity?

A
  • High H+ permeability
  • No ATPase activity
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9
Q

What are the 3 states of beta subunits in ATP synthase?

A

Tight, Loose, Open

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10
Q

What can the loose state of beta ATP synthase subunits bind to?

A

ADP + Pi

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11
Q

What brings about gamma subunit rotation in ATP synthase?

A

Energy from H+ transport

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12
Q

What occurs the gamma subunit is rotated in ATP synthase?

A
  • Tight state becomes the open state
  • Loose state becomes the tight state
  • Open state becomes the loose state
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13
Q

When the subunit which was previously tight is now open in ATP synthase what happens?

A

ATP is free to leave and ADP and Pi spontaneously form ATP

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14
Q

In ATP synthase is energy required for ATP synthesis?

A

No

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15
Q

In ATP synthase is energy required for ATP release?

A

Yes

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16
Q

What mechanism of energy transduction occurs in F1FO ATPase?

A

Indirect

17
Q

Conformational switching from the rotation of gamma subunit against alpha3beta3 moves how many degrees in which direction?

A

120º clockwise

18
Q

What does the c-ring of ATPase rotate with?

A

Gamma subunit

19
Q

What is the rotation of c-ring in ATPase driven by?

A

PMF

20
Q

What conserved residue is found in the c subunit of ATPase?

A

Glutamate

21
Q

What forms the stator of ATPase?

A

Peripheral stalk

22
Q

Movement of ATP,ADP, and Pi requires how many extra H+ from the PMF?

A

1

23
Q

What interaction does the conserved Glu form in ATPase C ring?

A

Salt bridge with Arg residue in alpha subunit

24
Q

What neutralises the Glu-Arg salt bridge in c ring of ATPase?

A

Protonation of Glu through a channel to P side

25
Q

In C-ring of ATPase what happens when Glu interaction has been neutralised?

A

Ring rotates so the next non-protonated c-subunit interacts with Arg-residue

26
Q

In C-ring of ATPase how are protons released to the N side?

A
  • C-ring rotates
  • At some point the protonated c-subunit aligns with a 2nd channel to the N-side
27
Q

In C-ring of ATPase what does 1 full rotation require?

A

H+ transfer through each c-subunit