Three-color Förster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time.

@article{Ernst2012ThreecolorFR,
  title={Three-color F{\"o}rster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time.},
  author={Stefan Ernst and Monika G. D{\"u}ser and Nawid Zarrabi and Michael B{\"o}rsch},
  journal={Journal of biomedical optics},
  year={2012},
  volume={17 1},
  pages={
          011004
        }
}
Catalytic activities of enzymes are associated with elastic conformational changes of the protein backbone. Förster-type resonance energy transfer, commonly referred to as FRET, is required in order to observe the dynamics of relative movements within the protein. Förster-type resonance energy transfer between two specifically attached fluorophores provides a ruler with subnanometer resolution between 3 and 8 nm, submillisecond time resolution for time trajectories of conformational changes… 
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Regulatory conformational changes of the Ɛ subunit in single FRET-labeled F0F1-ATP synthase

TLDR
An experimental system is developed that can reveal conditions under which ε inhibits the holoenzyme FoF1-ATP synthase in vitro and labels the C-terminal domain of ε and the γ subunit specifically with two different fluorophores for single-molecule Förster resonance energy transfer (smFRET).

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TLDR
A single-molecule FRET approach using duty cycle-optimized alternating laser excitation and new FRET transition histograms were developed to identify the smaller step sizes compared to the 10-stepped Fo motor of the Escherichia coli enzyme, indicating a high flexibility in the membrane part of this thermophilic enzyme.

Subunit rotation in single FRET-labeled F1-ATPase hold in solution by an anti-Brownian electrokinetic trap

TLDR
Monte Carlo simulations are used to reveal that stepwise FRET efficiency changes can be analyzed by Hidden Markov Models even at the limit of a low signal-to-background ratio that was expected due to high background count rates caused by the microfluidics of the ABELtrap.

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

TLDR
The novel FRET donor mNeonGreen is evaluated as a fusion to FoF1-ATP synthase and compare it to the previously used fluorophore EGFP to evaluate the biochemical purification procedures and activity measurements of the fully functional mutant enzyme.

The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL trap

TLDR
This work labels F1 specifically with two fluorophores to monitor the C-terminus of the ε subunit by Förster resonance energy transfer and compares FRET changes in single F1 and FRET histograms for different biochemical conditions to evaluate the proposed regulatory mechanism.

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