(Q44090533)

29 November 2017

title

Coupled rotation within single F0F1 enzyme complexes during ATP synthesis or hydrolysis (English)

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29 November 2017

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29 November 2017

Georg Kaim

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29 November 2017

Beate Sick

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29 November 2017

Gert Zumofen

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29 November 2017

Alois Renn

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29 November 2017

Urs P Wild

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29 November 2017

Peter Dimroth

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29 November 2017

language of work or name

English

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publication date

1 August 2002

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29 November 2017

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29 November 2017

volume

525

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29 November 2017

issue

1-3

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29 November 2017

page(s)

156-163

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Molecular architecture of the rotary motor in ATP synthase

29 November 2017

cites work

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https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903097-1

Bacterial Na(+)-ATP synthase has an undecameric rotor

21 January 2018

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Structural biology. Proton-powered turbine of a plant motor

21 January 2018

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

21 January 2018

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

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ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

21 January 2018

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Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation.

21 January 2018

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Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex.

21 January 2018

1 reference

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Functional and idling rotatory motion within F1-ATPase

21 January 2018

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Direct observation of the rotation of F1-ATPase

21 January 2018

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https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903097-1

Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging

21 January 2018

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Direct observation of the rotation of epsilon subunit in F1-ATPase

21 January 2018

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F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps

21 January 2018

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

21 January 2018

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Reconstitution of Fo of the sodium ion translocating ATP synthase of Propionigenium modestum from its heterologously expressed and purified subunits

21 January 2018

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F1-ATPase: a rotary motor made of a single molecule

21 January 2018

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Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase

21 January 2018

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Inter-subunit rotation and elastic power transmission in F0F1-ATPase.

21 January 2018

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Voltage-generated torque drives the motor of the ATP synthase

21 January 2018

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ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage

21 January 2018

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Energy transduction in the sodium F-ATPase of Propionigenium modestum

21 January 2018

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Intersubunit rotation in active F-ATPase

21 January 2018

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Three-stepped rotation of subunits gamma and epsilon in single molecules of F-ATPase as revealed by polarized, confocal fluorometry

21 January 2018

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Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

7 January 2021

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F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1)

7 January 2021

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NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles

7 January 2021

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Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy

7 January 2021

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Single-Molecule Identification by Spectrally and Time-Resolved Fluorescence Detection

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903097-1

Observations of rotation within the F(o)F(1)-ATP synthase: deciding between rotation of the F(o)c subunit ring and artifact

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2802%2903097-1

ATP synthesis by the F1Fo ATP synthase of Escherichia coli is obligatorily dependent on the electric potential

7 January 2021

1 reference

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10.1016/S0014-5793(02)03097-1

7 January 2021

Identifiers

DOI

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29 November 2017

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