Biology – Quantitative Biology – Biomolecules
Scientific paper
2012-01-30
Biology
Quantitative Biology
Biomolecules
14 pages, 7 figures
Scientific paper
The enzyme FoF1-ATP synthase provides the 'chemical energy currency' adenosine triphosphate (ATP) for living cells. Catalysis is driven by mechanochemical coupling of subunit rotation within the enzyme with conformational changes in the three ATP binding sites. Proton translocation through the membrane-bound Fo part of ATP synthase powers a 10-step rotary motion of the ring of c subunits. This rotation is transmitted to the gamma and epsilon subunits of the F1 part. Because gamma and epsilon subunits rotate in 120 deg steps, we aim to unravel this symmetry mismatch by real time monitoring subunit rotation using single-molecule Forster resonance energy transfer (FRET). One fluorophore is attached specifically to the F1 motor, another one to the Fo motor of the liposome-reconstituted enzyme. Photophysical artifacts due to spectral fluctuations of the single fluorophores are minimized by a previously developed duty cycle-optimized alternating laser excitation scheme (DCO-ALEX). We report the detection of reversible elastic deformations between the rotor parts of Fo and F1 and estimate the maximum angular displacement during the load-free rotation using Monte Carlo simulations
Boersch Michael
Dueser Monika G.
Ernst Stefan
Zarrabi Nawid
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