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

Fo is a water insoluble protein with eight subunits and transmembrane ring. The ring has a tetramer shape with protein helix circle helix that goes however conformational change when protonated and deprotonated permitting to push neighboring subunits to turn causing the turning of FO which at that point influences compliance of F1 likewise, coming about on exchanging of conditions of alpha and beta subunits. The FO area of ATP synthase is a proton pore that is inserted in the mitochondrial layer.

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