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Rotary catalysis of F(o)F(1)-ATP synthase

The synthesis of ATP, the key reaction of biological energy metabolism, is accomplished by the rotary motor protein; F(o)F(1)-ATP synthase (F(o)F(1)). In vivo, F(o)F(1,) located on the cell membrane, carries out ATP synthesis by using the proton motive force. This heterologous energy conversion is s...

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Detalles Bibliográficos
Autor principal: Watanabe, Rikiya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4629669/
https://www.ncbi.nlm.nih.gov/pubmed/27493540
http://dx.doi.org/10.2142/biophysics.9.51
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author Watanabe, Rikiya
author_facet Watanabe, Rikiya
author_sort Watanabe, Rikiya
collection PubMed
description The synthesis of ATP, the key reaction of biological energy metabolism, is accomplished by the rotary motor protein; F(o)F(1)-ATP synthase (F(o)F(1)). In vivo, F(o)F(1,) located on the cell membrane, carries out ATP synthesis by using the proton motive force. This heterologous energy conversion is supposed to be mediated by the mechanical rotation of F(o)F(1); however, it still remained unclear. Recently, we developed the novel experimental setup to reproduce the proton motive force in vitro and succeeded in directly observing the proton-driven rotation of F(o)F(1). In this review, we describe the interesting working principles determined so far for F(o)F(1) and then introduce results from our recent study.
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spelling pubmed-46296692016-08-04 Rotary catalysis of F(o)F(1)-ATP synthase Watanabe, Rikiya Biophysics (Nagoya-shi) Review Article The synthesis of ATP, the key reaction of biological energy metabolism, is accomplished by the rotary motor protein; F(o)F(1)-ATP synthase (F(o)F(1)). In vivo, F(o)F(1,) located on the cell membrane, carries out ATP synthesis by using the proton motive force. This heterologous energy conversion is supposed to be mediated by the mechanical rotation of F(o)F(1); however, it still remained unclear. Recently, we developed the novel experimental setup to reproduce the proton motive force in vitro and succeeded in directly observing the proton-driven rotation of F(o)F(1). In this review, we describe the interesting working principles determined so far for F(o)F(1) and then introduce results from our recent study. The Biophysical Society of Japan (BSJ) 2013-05-22 /pmc/articles/PMC4629669/ /pubmed/27493540 http://dx.doi.org/10.2142/biophysics.9.51 Text en ©2013 THE BIOPHYSICAL SOCIETY OF JAPAN
spellingShingle Review Article
Watanabe, Rikiya
Rotary catalysis of F(o)F(1)-ATP synthase
title Rotary catalysis of F(o)F(1)-ATP synthase
title_full Rotary catalysis of F(o)F(1)-ATP synthase
title_fullStr Rotary catalysis of F(o)F(1)-ATP synthase
title_full_unstemmed Rotary catalysis of F(o)F(1)-ATP synthase
title_short Rotary catalysis of F(o)F(1)-ATP synthase
title_sort rotary catalysis of f(o)f(1)-atp synthase
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4629669/
https://www.ncbi.nlm.nih.gov/pubmed/27493540
http://dx.doi.org/10.2142/biophysics.9.51
work_keys_str_mv AT watanaberikiya rotarycatalysisoffof1atpsynthase