Plant Phys exam 3: 4 ATP synthesis

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5 Terms

1
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Describe the structure of ATP synthase

alpha and beta- active site for ATP synthesis

beta- catalytic site

b- prevents alpha and beta from moving

Y- attached to c-ring, Y rotates as C ring rotates… between alpha and beta subunits

c- (c-ring) 8-14 subunits; H+ binding site, rotates 30-36 degrees when binging to C ring

a- H+ movement… H+ entrance from lumen/ H+ exit to stroma

<p>alpha and beta- active site for ATP synthesis</p><p>beta- catalytic site</p><p>b- prevents alpha and beta from moving</p><p>Y- attached to c-ring, Y rotates as C ring rotates… between alpha and beta subunits</p><p>c- (c-ring) 8-14 subunits; H+ binding site, rotates 30-36 degrees when binging to C ring</p><p>a- H+ movement… H+ entrance from lumen/ H+ exit to stroma</p>
2
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How do protons flow through ATP synthase?

H+ enter and exit ATP Synthase via the a subunit

  • H+ binding to C subunits causes rotation of ring (≅ 30-36 degrees)

  • C ring rotation causes rotation of 𝛄 subunit

  • 𝛄 rotation changes conformational of catalytic site in B subunits and drives the synthesis of ATP

  • Head unit does not rotate – its static

  • (and held in place by b and 𝜹)

3
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What influence does the H+ concentration have on ATP synthase?

higher concentration= more likely to bind

lower concentration= more likely to dissociate

4
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Which subunit in ATP synthase is variable amongst organisms?

C ring subunit

5
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What is rational catalysis?

For each beta subunit (β) the active site can exists as O (open) L (loose) T (tight) conformations

  • Proton flow and rotation of asymmetric gamma subunit changes the conformation

  • 3 ATP/360 degree rotation of gamma subunit