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Two decades ago, we introduced single-molecule FRET measurements to study subunit rotation in individual FoF1-ATP synthases in liposomes. The rotary motors of the enzyme are either driven by ATP hydrolysis, or by internal proton translocation. To counteract diffusive motion of a single enzyme in real time, we built a fast confocal anti-Brownian electrokinetic trap (invented by A. E. Cohen and W. E. Moerner) with laser focus pattern and electrode feedback. We recorded broad distributions of ATP-driven subunit rotation and changing rotor speed in time traces of single enzymes. Now we explore the speed limit by circumventing the biological regulatory controls.
Michael Börsch,Thomas Heitkamp, andIván Pérez
"20 years of happy motoring with single FoF1-ATP synthase: exploring the speed limit (Conference Presentation)", Proc. SPIE PC12386, Single Molecule Spectroscopy and Superresolution Imaging XVI, PC1238602 (15 March 2023); https://doi.org/10.1117/12.2648056
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Michael Börsch, Thomas Heitkamp, Iván Pérez, "20 years of happy motoring with single FoF1-ATP synthase: exploring the speed limit (Conference Presentation)," Proc. SPIE PC12386, Single Molecule Spectroscopy and Superresolution Imaging XVI, PC1238602 (15 March 2023); https://doi.org/10.1117/12.2648056