ATP synthase is a large molecular machine that converts the energy in an electrochemical gradient into the bond energy stored in ATP. Which of the following events are required for the synthesis of ATP? Choose one or more:A.binding of ATP to an empty F1 ATPase subunitB.rotation of the rotor in the membraneC.conformational changes of the F1 ATPaseD.movement of protons down their gradient through ATP synthase Part 2(1 pt) See Hint Suppose the shaft of ATP synthase that is attached to the rotor were truncated (shortened) such that it no longer extended into the F1 ATPase head. What would be the consequence of this mutation? Choose one:A. The rotor in the membrane would no longer turn.B. ATP would not be produced because the conformation of the F1 ATPase head would not be changed.C. Protons would not cross the membrane using the rotor.D. ATP synthase would work in reverse, breaking down ATP and pumping protons against their gradient.
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Part 1: Events Required for the Synthesis of ATP ** Show more…
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Suppose the shaft of ATP synthase that is attached to the rotor were truncated (shortened) such that it no longer extended into the F1 ATPase head. What would be the consequence of this mutation? A. Protons would not cross the membrane using the rotor. B. The rotor in the membrane would no longer turn C. ATP would not be produced because the conformation of the F1 ATPase head would not be changed .D. ATP synthase would work in reverse, breaking down ATP and pumping protons against their gradient.
Madhur L.
1. The number of protons transferred across the membrane during a complete rotation of the F1-γ subunit is equal to the number of Fo-c subunits in the Fo-c ring. 2. While catalyzing ATP synthesis, each nucleotide-binding site in the F1 portion will cycle through the 3 conformational states in this order: T→L→O. 3. The function of the Fo-b subunit ('stator') is to keep the F1-α3β3 hexamer from rotating with F1-γ. 4. The F1-γ subunit and Fo-c ring rotate in opposite directions. 5. Protons get to and from the Fo-c subunit via half-channels in the Fo-a subunit. 6. Rotation of the Fo-c ring is driven by proton transport across the membrane due to electrostatic repulsion of the protons with positively charged residues in the Fo-c subunits. 7. Phosphorylation of ADP is driven essentially by binding energy: the T (tight) conformation binds ATP with very high affinity.
Md.Daniyal A.
Select all that apply What true about the conformational aspects of coupling? The proton gradient is involved in the release 0f bound ATP from the synthase as result of conformational change. The conformational states interconvert a5 result of proton flux through the synthase There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis The Fo portion of ATP synthase acts as rotary motor
Adi S.
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