Respuesta :
ATP is formed in the F 1 sector of the enzyme, synthesis is driven by rotation of the γ subunit between three alternating catalytic sites.
The rotational catalytic process used by F1F0 ATP synthases to produce ATP involves the coupling of H+ transport and rotation of an oligomeric ring of c subunits that extends through the membrane. At the membrane's core, protons bind to and subsequently are released from the aspartyl-61 residue of subunit c. It is believed that subunit an of the F0 sector offers proton access routes to and from aspartyl-61. Here, we provide a summary of recent findings regarding the second, fourth, and fifth transmembrane helices' aqueous accessibility and the structural layout of Escherichia coli subunit a. (TMHs). These helices have aqueous-accessible areas that reach the cytoplasmic and periplasmic surfaces. We suggest that during the proton transport cycle, aTMH4 rotates to alternatively expose the periplasmic or cytoplasmic half-channels to aspartyl-61 of subunit c. According to a mechanism resembling mesh gears, it is proposed that the mechanical force driving rotation of the c-rotor is the coordinated rotation of interacting helices in subunits a and c.
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