Figure 1
From: The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
The experimental system. Cyt. bo 3 and ATP-synthase from E. coli were co-reconstituted in vesicles (a part of the membrane is shown). For measurements of protein-protein interactions, cyt. bo 3 and ATP-synthase were labeled with fluorophores (not shwon, see text). To measure the coupled activity, DTT and quinone were added, which initiates transmembrane proton transfer, driven by the quinol oxidase. The ATP-synthesis rate was monitored by measuring changes in luminescence that originates from added luciferase/luciferin. Proton transfer along the membrane surface is discussed in the Discussion section.
