José D. Faraldo-Gómez

TL;DR: It is proposed that the assembly of ATP synthase dimer rows is driven by the reduction in the membrane elastic energy, rather than by direct protein contacts, and that the dimerrows enable the formation of highly curved ridges in mitochondrial cristae.

TL;DR: A model for proton translocation whereby the c subunits remain in this proton-locked state when facing the membrane lipid is proposed, and the different coordination chemistry of the bound proton and the smaller curvature of the outer helix drastically enhance the selectivity of the H+ site against other cations, including H3O+.

TL;DR: Evidence is presented supporting the notion that the ability of c-rings to rotate within the F(o) complex derives from the interplay between the ion-binding sites and their nonhomogenous microenvironment, and how the thermodynamic stability of the so-called proton-locked state is maximized by the lipid membrane.

TL;DR: It is proposed that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release, and is a consequence of the amphiphilic nature of the crystallization buffer.

TL;DR: This work studies the methanogenic archaeon Methanosarcina acetivorans using assays of ATP hydrolysis and ion transport in inverted membrane vesicles, and experimentally demonstrates that the rotary mechanism of its ATP synthase is coupled to the concurrent translocation of both H+ and Na+ across the membrane under physiological conditions.