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Adenosine triphosphate (ATP) is the universal chemical energy currency forcellular activities provided mainly by the membrane enzyme FoF1-ATP synthase inbacteria, chloroplasts and mitochondria. Synthesis of ATP is accompanied bysubunit rotation within the enzyme. Over the past 15 years we have developed avariety of single-molecule FRET (smFRET) experiments to monitor catalyticaction of individual bacterial enzymes in vitro. By specifically labelingrotating and static subunits within a single enzyme we were able to observethree-stepped rotation in the F1 motor, ten-stepped rotation in the Fo motorand transient elastic deformation of the connected rotor subunits. However, thespatial and temporal resolution of motor activities measured by smFRET werelimited by the photophysics of the FRET fluorophores. Here we evaluate thenovel FRET donor mNeonGreen as a fusion to FoF1-ATP synthase and compare it tothe previously used fluorophore EGFP. Topics of this manuscript are thebiochemical purification procedures and the activity measurements of the fullyfunctional mutant enzyme.

Observing single FoF1-ATP synthase at work using an improved fluorescent protein mNeonGreen as FRET donor