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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Biophysical Society of Japan (BSJ)
2013
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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. |
format | Online Article Text |
id | pubmed-4629669 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
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 |