Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues.

F₁F_o-ATP synthase is a multisubunit enzyme responsible for the synthesis of ATP. Among its multiple subunits (8 in E. coli, 17 in yeast S. cerevisiae, 16 in vertebrates), two subunits a and c are known to play a central role controlling the H⁺ flow through the inner mitochondrial membrane which allows the subsequent synthesis of ATP, but the pathway followed by H⁺ within the two proteins is still a matter of debate. In fact, even though the structure of ATP synthase is now well defined, the molecular mechanisms determining the function of both F₁ and F_O domains are still largely unknown. In this study, we propose a pathway for proton migration along the ATP synthase by hydrogen-bonded chain mechanism, with a key role of serine and threonine residues, by X-ray diffraction data on the subunit a of E. coli Fo.

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