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Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B.
36° step size of proton‐driven c‐ring rotation in FoF1‐ATP synthase
Using single‐molecule fluorescence resonance energy transfer, this work provides the first experimental determination of a 36° sequential stepping mode of the c‐ring during ATP synthesis.
Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer.
Monitoring the rotary motors of single FoF1-ATP synthase by synchronized multi channel TCSPC
The action mode of bactericidal drugs, i.e. inhibitors of FoF1-ATP synthase like aurovertin, could be investigated by the time resolved single-molecule FRET approach.
The Proton-translocating a Subunit of F0F1-ATP Synthase Is Allocated Asymmetrically to the Peripheral Stalk*
- M. Düser, Y. Bi, N. Zarrabi, S. Dunn, M. Börsch
- Biology, ChemistryJournal of Biological Chemistry
- 28 November 2008
The position of the a subunit of the membrane-integral F0 sector of Escherichia coli ATP synthase was investigated, finding that this relationship provides stability to the membrane interface between a and b2, allowing it to withstand the torque imparted by the rotor during ATP synthesis as well as ATP hydrolysis.
Simultaneous monitoring of the two coupled motors of a single FoF1-ATP synthase by three-color FRET using duty cycle-optimized triple-ALEX
To reduce photophysical artifacts due to spectral fluctuations of the single fluorophores, a duty cycle-optimized alternating three-laser scheme (DCO-ALEX) has been developed and simultaneous observation of the stepsizes for both motors allows the detection of reversible elastic deformations between the rotor parts of Fo and F1.
Three-color Förster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time.
This work presents a new single-molecule FRET approach to observe both rotary motors simultaneously in a single F(O)F(1)-ATP synthase at work, and labels this enzyme with three fluorophores, specifically at the stator part and at the two rotors.
Quantum dots for single-pair fluorescence resonance energy transfer in membrane- integrated EFoF1.
- E. Galvez, M. Düser, M. Börsch, J. Wrachtrup, P. Gräber
- ChemistryBiochemical Society transactions
- 1 October 2008
TIRFM (total internal reflection microscopy) shows that covalent binding of the QD (quantum dot) via cysteine to FoF1 leads to a significant decrease in the blinking probability in the microsecond-to-second time range.
3D-localization of the a-subunit in F0F1-ATP synthase by time resolved single-molecule FRET
- M. Düser, N. Zarrabi, Y. Bi, B. Zimmermann, S. Dunn, M. Börsch
- Biology, ChemistrySPIE BiOS
- 27 February 2006
Rotation of the ε-subunit during ATP hydrolysis was divided into three major steps and the stopping positions of ε resulted in three distinct FRET efficiency levels and FRET donor lifetimes and the position of the FRET donors at the asubunit was calculated.
36 1 step size of proton-driven c-ring rotation in FoF 1-ATP synthase
Using single-molecule fluorescence resonance energy transfer, this work provides the first experimental determination of a 361 sequential stepping mode of the c-ring during ATP synthesis.