Literature DB >> 23395605

Chemomechanical coupling mechanism of F(1)-ATPase: catalysis and torque generation.

Rikiya Watanabe1, Hiroyuki Noji.   

Abstract

F1-ATPase (F1), a rotary motor protein driven by ATP hydrolysis, is unique with respect to its high efficiency and reversibility in converting chemical energy into mechanical work. Single-molecule studies have improved our understanding about the energy-conversion mechanism of F1 and the chemomechanical-coupling scheme under ATP hydrolysis conditions. A novel single-molecule technique was recently established to estimate the free-energy change of F1 during catalysis at elementary-step resolution, advancing our understanding about the energy-conversion mechanism of ATP hydrolysis and synthesis. The energy conversion mechanism of F1 elucidated from single-molecule studies provides us with important insights into the operating principles underlying molecular motors.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2013        PMID: 23395605     DOI: 10.1016/j.febslet.2013.01.063

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  18 in total

1.  Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.

Authors:  Edgar Morales-Rios; Martin G Montgomery; Andrew G W Leslie; John E Walker
Journal:  Proc Natl Acad Sci U S A       Date:  2015-10-12       Impact factor: 11.205

2.  Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.

Authors:  Sándor Volkán-Kacsó; Rudolph A Marcus
Journal:  Proc Natl Acad Sci U S A       Date:  2015-10-19       Impact factor: 11.205

3.  Catalysis-enhancement via rotary fluctuation of F1-ATPase.

Authors:  Rikiya Watanabe; Kumiko Hayashi; Hiroshi Ueno; Hiroyuki Noji
Journal:  Biophys J       Date:  2013-11-19       Impact factor: 4.033

Review 4.  Opposite rotation directions in the synthesis and hydrolysis of ATP by the ATP synthase: hints from a subunit asymmetry.

Authors:  Salvatore Nesci; Fabiana Trombetti; Vittoria Ventrella; Alessandra Pagliarani
Journal:  J Membr Biol       Date:  2015-02-06       Impact factor: 1.843

5.  Torque transmission mechanism via DELSEED loop of F1-ATPase.

Authors:  Rikiya Watanabe; Kazuma Koyasu; Huijuan You; Mizue Tanigawara; Hiroyuki Noji
Journal:  Biophys J       Date:  2015-03-10       Impact factor: 4.033

6.  Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites.

Authors:  Nelli Mnatsakanyan; Yunxiang Li; Joachim Weber
Journal:  J Biol Chem       Date:  2018-12-03       Impact factor: 5.157

7.  Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPase.

Authors:  Sándor Volkán-Kacsó; Rudolph A Marcus
Journal:  Proc Natl Acad Sci U S A       Date:  2016-10-10       Impact factor: 11.205

Review 8.  Multiscale molecular dynamics simulations of rotary motor proteins.

Authors:  Toru Ekimoto; Mitsunori Ikeguchi
Journal:  Biophys Rev       Date:  2017-12-04

9.  Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase.

Authors:  Rikiya Watanabe; Makoto Genda; Yasuyuki Kato-Yamada; Hiroyuki Noji
Journal:  Biophys J       Date:  2018-01-09       Impact factor: 4.033

10.  Structure of the mitochondrial ATP synthase from Pichia angusta determined by electron cryo-microscopy.

Authors:  Kutti R Vinothkumar; Martin G Montgomery; Sidong Liu; John E Walker
Journal:  Proc Natl Acad Sci U S A       Date:  2016-10-24       Impact factor: 11.205

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