The beta-subunit of ATP synthase can assume three different conformational state

Question

The beta-subunit of ATP synthase can assume three different conformational states: loose affinity binding, high affinity binding, and an empty state. What process drives the conformational change from a high affinity state to an empty state during the synthesis of ATP? Electrons flowing through the Fo complex cause a conformational change in the c-subunit of Fo, and this drives the change from a high affinity state to an empty state. Protons flowing through the Fo complex drive a rotational change in the gamma-subunit of F1, and this drives the change from a high affinity state to an empty state. The conformation change from a high affinity state to an empty state is driven by the energy of ATP binding. The beta-subunits migrate from the matrix to the inner membrane space, and the energy of this process drives the conformational change.

Explanation / Answer

Q.the beta subunit of the atp synthase can assume three different conformational states: loose affinity binding. High affinity binding, and an empty state. What process drivers the conformational change from a high affinity state to an empty state during the synthesis of ATP?

ans: Protons flowing through the Fo complex drive rotational changes in the gamma-subunit of F1, and this drives the change from a high affinity state to an empty state.

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