activity
20072012
most cited36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase

22 citations · 83 across the 9 of their papers we have counts for

collaborators
Showing q-bio.BMShow all

6 papers · 1 filter

q-bio.BM2012★ 3 cited

Step size of the rotary proton motor in single FoF1-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET

Eva Hammann, Andrea Zappe, Stefanie Keis +5

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 co…

q-bio.BM2012★ 3 cited

Monitoring transient elastic energy storage within the rotary motors of single FoF1-ATP synthase by DCO-ALEX FRET

Stefan Ernst, Monika G. Dueser, Nawid Zarrabi +1

The enzyme FoF1-ATP synthase provides the 'chemical energy currency' adenosine triphosphate (ATP) for living cells. Catalysis is driven by mechanochemical coupling of subunit rotat…

q-bio.BM2011★ 7 cited

Subunit rotation in a single FoF1-ATP synthase in a living bacterium monitored by FRET

Karin Seyfert, Takuya Oosaka, Hideyuki Yaginuma +4

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

q-bio.BM2011★ 4 cited

Drug transport mechanism of P-glycoprotein monitored by single molecule fluorescence resonance energy transfer

Stefan Ernst, Brandy Verhalen, Nawid Zarrabi +2

In this work we monitor the catalytic mechanism of P-glycoprotein (Pgp) using single-molecule fluorescence resonance energy transfer (FRET). Pgp, a member of the ATP binding casset…

q-bio.BM2009★ 22 cited

36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase

Monika G. Dueser, Nawid Zarrabi, Daniel J. Cipriano +4

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 ro…

q-bio.BM2009★ 15 cited

Simultaneous monitoring of the two coupled motors of a single FoF1-ATP synthase by three-color FRET using duty cycle-optimized triple-ALEX

N. Zarrabi, S. Ernst, M. G. Dueser +5

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 inter…