Question 14 of 20 A mutation in human ATPase 6, which corresponds to E. coli subunit a, from leucine to arginine at position 156 may allow the movement of protons across the membrane, but not the rotation of the ring of c subunits. How might this possible mechanism affect the function of ATP synthase? Choose two answers. There would be no net effect on the overall function of ATP synthase. There would be an uncoupling of proton translocation and ATP synthesis. The c ring would become uncoupled from the γ and ε subunits. ATP hydrolysis coupled to proton transport out of the matrix would increase. Proton binding to subunit c would be impaired. ATP synthase would remain sensitive to F0 proton conduction inhibitors.

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Wall

Biology

13 May, 10:11

Question 14 of 20 A mutation in human ATPase 6, which corresponds to E. coli subunit a, from leucine to arginine at position 156 may allow the movement of protons across the membrane, but not the rotation of the ring of c subunits. How might this possible mechanism affect the function of ATP synthase? Choose two answers. There would be no net effect on the overall function of ATP synthase. There would be an uncoupling of proton translocation and ATP synthesis. The c ring would become uncoupled from the γ and ε subunits. ATP hydrolysis coupled to proton transport out of the matrix would increase. Proton binding to subunit c would be impaired. ATP synthase would remain sensitive to F0 proton conduction inhibitors.

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Kara Neal · Answer 1

The answers are the following:

1 - There would be an uncoupling of proton translocation and ATP synthesis.

2 - ATP synthase would remain sensitive to F0 proton conduction inhibitors.