Fig. 4: Biophysical characterisation of proton conduction properties in dissected antiporter-like modules co-reconstituted with F1Fo-ATP synthase. | Nature Communications

Fig. 4: Biophysical characterisation of proton conduction properties in dissected antiporter-like modules co-reconstituted with F1Fo-ATP synthase.

From: Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I

Fig. 4

a Proteoliposome assay for probing the proton conduction kinetics in the dissected antiporter-like subunits co-reconstituted with ATP synthase, monitored by fluorescence quenching of ACMA. Addition of 0.2 mM ATP generates an ATPase-driven ∆pH across the proteoliposome membrane, which competes with the (d) Nqo12 ΔTH- and (f) Nqo13-mediated proton transport. b, c Structure of the proton pathways from MD simulations of the WT (blue) and ion-pair mutants (orange) for (b) Nqo12ΔTH and (c) Nqo13. Sidechains of conserved residues are shown as sticks, water molecules as spheres. Relative ACMA quenching amplitudes for co-reconstituted ATP synthase with (e) Nqo12∆TH and (g) Nqo13 constructs. Data shown are derived from independent experiments where n = 6 (mean ± SD), except F1Fo-K235M13 where n = 5. Data are provided in the Source Data file.

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