36° step size of proton-driven c-ring rotation in FoF1-ATP synthase-Reference-Cited by-同舟云学术

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

Published:2009-07-30 Issue:18 Volume:28 Page:2689-2696
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Düser Monika G,Zarrabi Nawid,Cipriano Daniel J,Ernst Stefan,Glick Gary D,Dunn Stanley D,Börsch Michael

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference37 articles.

1. Rotation of a γ-ε Subunit Domain in the Escherichia coli F1F0-ATP Synthase Complex

2. Insights into the Molecular Mechanism of Rotation in the Fo Sector of ATP Synthase

3. Separating Structural Heterogeneities from Stochastic Variations in Fluorescence Resonance Energy Transfer Distributions via Photon Distribution Analysis

4. Constant c 10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking

5. Stepwise rotation of the γ-subunit of EF0F1-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer1

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1. Single NV center in nanodiamond for quantum sensing of protein dynamics in an ABEL trap;Single Molecule Spectroscopy and Superresolution Imaging XVII;2024-03-12

2. The ATPase asymmetry: Novel computational insight into coupling diverse FO motors with tripartite F1;Biophysical Journal;2024-03

3. Single NV in nanodiamond for quantum sensing of protein dynamics in an ABEL trap;2024-01-25

4. Directed proton transfer from Fo to F1 extends the multifaceted proton functions in ATP synthase;Biophysical Reviews;2023-09-21

5. Mechanism of ADP-Inhibited ATP Hydrolysis in Single Proton-Pumping FoF1-ATP Synthase Trapped in Solution;International Journal of Molecular Sciences;2023-05-08

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