A mutation in human ATPase 6, which corresponds to E. coli subunit a, from leucine to arginine at position 156 may allow the mov
ement of protons across the membrane, but not the rotation of the ring of c subunits.
1 answer:
Answer:
There would be the uncoupling of proton translocation and ATP synthesis.
There would be no net effect on the overall function of ATP synthase.
ATP hydrolysis coupled to proton transport out of the matrix would increase.
ATP synthase would remain sensitive to F0 proton conduction inhibitors.
Proton binding to sub-unit c would be impaired.
The c sub-units would not fold correctly.
Explanation:
- There would be the uncoupling of proton translocation and ATP synthesis.
- There would be no net effect on the overall function of ATP synthase.
- ATP hydrolysis coupled to proton transport out of the matrix would increase.
- ATP synthase would remain sensitive to F0 proton conduction inhibitors.
- Proton binding to sub-unit c would be impaired.
- The c sub-units would not fold correctly.
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