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Related papers: 3D-localization microscopy and tracking of FoF1-AT…

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FoF1-ATP synthases in Escherichia coli (E. coli) bacteria are membrane-bound enzymes which use an internal proton-driven rotary double motor to catalyze the synthesis of adenosine triphosphate (ATP). According to the 'chemiosmotic…

Biological Physics · Physics 2015-06-04 Marc Renz , Torsten Rendler , Michael Boersch

Confocal time resolved single-molecule spectroscopy using pulsed laser excitation and synchronized multi channel time correlated single photon counting (TCSPC) provides detailed information about the conformational changes of a biological…

Biological Physics · Physics 2009-11-13 N. Zarrabi , M. G. Dueser , S. Ernst , R. Reuter , G. D. Glick , S. D. Dunn , J. Wrachtrup , M. Boersch

FoF1-ATP synthase is the ubiquitous membrane-bound enzyme in mitochondria, chloroplasts and bacteria which provides the 'chemical energy currency' adenosine triphosphate (ATP) for cellular processes. In Escherichia coli ATP synthesis is…

Biomolecules · Quantitative Biology 2015-05-27 Karin Seyfert , Takuya Oosaka , Hideyuki Yaginuma , Stefan Ernst , Hiroyuki Noji , Ryota Iino , Michael Boersch

FoF1-ATP synthase is the essential membrane enzyme maintaining the cellular level of adenosine triphosphate (ATP) and comprises two rotary motors. We measure subunit rotation in FoF1-ATP synthase by intramolecular Foerster resonance energy…

Quantitative Methods · Quantitative Biology 2015-05-27 Torsten Rendler , Marc Renz , Eva Hammann , Stefan Ernst , Nawid Zarrabi , Michael Boersch

FoF1-ATP synthase is the membrane protein catalyzing the synthesis of the 'biological energy currency' adenosine triphosphate (ATP). The enzyme uses internal subunit rotation for the mechanochemical conversion of a proton motive force to…

Biomolecules · Quantitative Biology 2015-06-15 Thomas Heitkamp , Hendrik Sielaff , Anja Korn , Marc Renz , Nawid Zarrabi , Michael Boersch

FoF1-ATP synthase is the enzyme that provides the 'chemical energy currency' adenosine triphosphate, ATP, for living cells. The formation of ATP is accomplished by a stepwise internal rotation of subunits within the enzyme. Briefly, proton…

Biomolecules · Quantitative Biology 2009-11-13 N. Zarrabi , S. Ernst , M. G. Dueser , A. Golovina-Leiker , W. Becker , R. Erdmann , S. D. Dunn , M. Borsch

F1-ATPase is the soluble portion of the membrane-embedded enzyme FoF1-ATP synthase that catalyzes the production of adenosine triphosphate in eukaryotic and eubacterial cells. In reverse, the F1 part can also hydrolyze ATP quickly at three…

Biomolecules · Quantitative Biology 2015-06-18 Samuel D. Bockenhauer , Thomas M. Duncan , W. E. Moerner , Michael Boersch

FoF1-ATP synthase is the enzyme that provides the 'chemical energy currency' adenosine triphosphate, ATP, for living cells. The formation of ATP is accomplished by a stepwise internal rotation of subunits within the enzyme. We monitor…

Biological Physics · Physics 2015-06-26 N. Zarrabi , M. G. Dueser , R. Reuter , S. D. Dunn , J. Wrachtrup , M. Boersch

Adenosine triphosphate (ATP) is the universal chemical energy currency for cellular activities provided mainly by the membrane enzyme FoF1-ATP synthase in bacteria, chloroplasts and mitochondria. Synthesis of ATP is accompanied by subunit…

Biomolecules · Quantitative Biology 2016-08-03 Thomas Heitkamp , Gabriele Deckers-Hebestreit , Michael Börsch

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…

Biomolecules · Quantitative Biology 2015-06-04 Stefan Ernst , Monika G. Dueser , Nawid Zarrabi , Michael Boersch

FoF1-ATP synthases are ubiquitous membrane-bound, rotary motor enzymes that can catalyze ATP synthesis and hydrolysis. Their enzyme kinetics are controlled by internal subunit rotation, by substrate and product concentrations, by mechanical…

Biomolecules · Quantitative Biology 2021-06-29 Thomas Heitkamp , Michael Börsch

Thermophilic enzymes can operate at higher temperatures but show reduced activities at room temperature. They are in general more stable during preparation and, accordingly, are considered to be more rigid in structure. Crystallization is…

Biomolecules · Quantitative Biology 2015-06-04 Eva Hammann , Andrea Zappe , Stefanie Keis , Stefan Ernst , Doreen Matthies , Thomas Meier , Gregory M. Cook , Michael Boersch

Synthesis of the biological "energy currency molecule" adenosine triphosphate ATP is accomplished by FoF1-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the Fo motor powers…

Biomolecules · Quantitative Biology 2009-03-03 Monika G. Dueser , Nawid Zarrabi , Daniel J. Cipriano , Stefan Ernst , Gary D. Glick , Stanley D. Dunn , Michael Boersch

Subunit epsilon is an intrinsic regulator of the bacterial FoF1-ATP synthase, the ubiquitous membrane-embedded enzyme that utilizes a proton motive force in most organisms to synthesize adenosine triphosphate (ATP). The C-terminal domain of…

Biomolecules · Quantitative Biology 2014-02-18 Thomas M. Duncan , Monika G. Dueser , Thomas Heitkamp , Duncan G. G. McMillan , Michael Boersch

We demonstrate asymmetric enzyme kinetics of a biomolecular motor F1-ATPase between synthesis and hydrolysis of adenosine triphosphate (ATP). Our experiments show that ATP hydrolysis follows Michaelis-Menten kinetics, but ATP synthesis,…

Biological Physics · Physics 2025-06-04 Yohei Nakayama , Shoichi Toyabe

FoF1-ATP synthase catalyzes the synthesis of adenosine triphosphate (ATP). The F1 portion can be stripped from the membrane-embedded Fo portion of the enzyme. F1 acts as an ATP hydrolyzing enzyme, and ATP hydrolysis is associated with…

Biomolecules · Quantitative Biology 2018-02-14 Hendrik Sielaff , Thomas Heitkamp , Andrea Zappe , Nawid Zarrabi , Michael Boersch

The life of a cell is governed by highly dynamical microscopic processes. Two notable examples are the diffusion of membrane receptors and the kinetics of transcription factors governing the rates of gene expression. Different fluorescence…

Quantitative Methods · Quantitative Biology 2020-04-03 Maxime Woringer , Ignacio Izeddin , Cyril Favard , Hugues Berry

To monitor conformational changes of individual membrane transporters in liposomes in real time, we attach two fluorophores to selected domains of a protein. Sequential distance changes between the dyes are recorded and analyzed by Forster…

Quantitative Methods · Quantitative Biology 2015-06-11 Bertram Su , Monika G. Dueser , Nawid Zarrabi , Thomas Heitkamp , Ilka Starke , Michael Börsch

F$_\mathrm{o}$F$_1$-ATP synthase is a factory for synthesizing ATP in virtually all cells. Its core machinery is the subcomplex F$_1$-motor (F$_1$-ATPase) and performs the reversible mechanochemical coupling. Isolated F$_1$-motor hydrolyzes…

Biological Physics · Physics 2015-01-19 Shoichi Toyabe , Eiro Muneyuki

Cytochrome C oxidase and FoF1-ATP synthase constitute complex IV and V, respectively, of the five membrane-bound enzymes in mitochondria comprising the respiratory chain. These enzymes are located in the inner mitochondrial membrane (IMM),…

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