Question

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.1. There would be an uncoupling of proton translocation and ATP synthesis.2. ATP hydrolysis coupled to proton transport out of the matrix would increase.3. There would be no net effect on the overall function of ATP synthase.4. ATP synthase would remain sensitive to F0 proton conduction inhibitors.5. The c subunits would not fold correctly.6. Proton binding to subunit c would be impaired.

Answer 1

1. There would be an uncoupling of proton translocation and ATP synthesis. 2. ATP synthase would remain sensitive to Fo proton conduction inhibitors.

Adenosine di phosphate (ADP) and inorganic phosphate are used to create the energy storage molecule adenosine triphosphate (ATP) by a protein called ATP synthase (Pi). It is categorized as a ligase since it modifies ADP by forming a P-O link (phosphodiester bond).

A molecular device called ATP synthase. Energy-wise, the production of ATP from ADP and Pi is undesirable, and the process would typically go the other way.

A proton (H+) concentration gradient across the inner mitochondrial membrane in eukaryotes or the plasma membrane in bacteria drives this reaction forward by coupling ATP synthesis during cellular respiration to the gradient.

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