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Movements of the ε‐subunit during catalysis and activation in single membrane‐bound H+‐ATP synthase
It is concluded that the active–inactive transition was associated with a conformational change of ε within the central stalk within F0F1‐ATP synthases, which catalyze proton transport‐coupled ATP synthesis in bacteria, chloroplasts, and mitochondria.
Detecting substeps in the rotary motors of FoF1-ATP synthase by Hidden Markov Models
The basic prerequisites for the experimental single-molecule FRET data are defined that allow for discrimination between a 120o stepping mode or a 36o substep rotation mode for the proton-driven Fo motor of ATP synthase.
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.
Asymmetry of rotational catalysis of single membrane-bound F0F1-ATP synthase
- N. Zarrabi, B. Zimmermann, M. Diez, P. Graeber, J. Wrachtrup, M. Boersch
- Chemistry, BiologySPIE BiOS
- 29 March 2005
Computer simulations of the FRET signals and non-equally distributed orientations of ε strongly corroborate asymmetry of catalysis in F0F1-ATP synthase.
Mechanistic basis for differential inhibition of the F1Fo‐ATPase by aurovertin
Single‐molecule experiments provide evidence that the residual rate of ATP hydrolysis seen in the presence of saturating concentrations of aurovertin results from a decrease in the binding change mechanism by hindering catalytic site interactions, which should further the understanding of how the F1Fo‐ATPase catalyzes ATP synthesis and hydrolyzing.
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.
Exploiting the nitrilotriacetic acid moiety for biolabeling with ultrastable perylene dyes.
- K. Peneva, G. Mihov, K. Müllen
- Chemistry, BiologyJournal of the American Chemical Society
- 23 April 2008
The solution and solid phase synthesis of water-soluble perylene(dicarboximide) functionalized with a nitrilotriacetic acid moiety (PDI-NTA) revealed an exceptional photostability and fluorescence quantum yield that remained unchanged upon addition of nickel ions.
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.
Movements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase.
It is concluded that the active-inactive transition was associated with a conformational change of epsilon within the central stalk of F0F1-ATP synthases, and the three states of the inactive enzyme were unequally populated.