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Importance of water entropy in rotation mechanism of F(1)-ATPase
We briefly review our theoretical study on the rotation scheme of F(1)-ATPase. In the scheme, the key factor is the water entropy which has been shown to drive a variety of self-assembly processes in biological systems. We decompose the crystal structure of F(1)-ATPase into three sub-complexes each...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Biophysical Society of Japan (BSJ)
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036781/ https://www.ncbi.nlm.nih.gov/pubmed/27857599 http://dx.doi.org/10.2142/biophysics.7.113 |
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author | Yoshidome, Takashi |
author_facet | Yoshidome, Takashi |
author_sort | Yoshidome, Takashi |
collection | PubMed |
description | We briefly review our theoretical study on the rotation scheme of F(1)-ATPase. In the scheme, the key factor is the water entropy which has been shown to drive a variety of self-assembly processes in biological systems. We decompose the crystal structure of F(1)-ATPase into three sub-complexes each of which is composed of the γ subunit, one of the β subunits, and two α subunits adjacent to them. The β(E), β(TP), and β(DP) subunits are involved in the sub-complexes I, II, and III, respectively. We calculate the hydration entropy of each sub-complex using a hybrid of the integral equation theory for molecular liquids and the morphometric approach. It is found that the absolute value of the hydration entropy follows the order, sub-complex I > sub-complex II > sub-complex III. Moreover, the differences are quite large, which manifests highly asymmetrical packing of F(1)-ATPase. In our picture, this asymmetrical packing plays crucially important roles in the rotation of the γ subunit. We discuss how the rotation is induced by the water-entropy effect coupled with such chemical processes as ATP binding, ATP hydrolysis, and release of the products. |
format | Online Article Text |
id | pubmed-5036781 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Biophysical Society of Japan (BSJ) |
record_format | MEDLINE/PubMed |
spelling | pubmed-50367812016-11-17 Importance of water entropy in rotation mechanism of F(1)-ATPase Yoshidome, Takashi Biophysics (Nagoya-shi) Review We briefly review our theoretical study on the rotation scheme of F(1)-ATPase. In the scheme, the key factor is the water entropy which has been shown to drive a variety of self-assembly processes in biological systems. We decompose the crystal structure of F(1)-ATPase into three sub-complexes each of which is composed of the γ subunit, one of the β subunits, and two α subunits adjacent to them. The β(E), β(TP), and β(DP) subunits are involved in the sub-complexes I, II, and III, respectively. We calculate the hydration entropy of each sub-complex using a hybrid of the integral equation theory for molecular liquids and the morphometric approach. It is found that the absolute value of the hydration entropy follows the order, sub-complex I > sub-complex II > sub-complex III. Moreover, the differences are quite large, which manifests highly asymmetrical packing of F(1)-ATPase. In our picture, this asymmetrical packing plays crucially important roles in the rotation of the γ subunit. We discuss how the rotation is induced by the water-entropy effect coupled with such chemical processes as ATP binding, ATP hydrolysis, and release of the products. The Biophysical Society of Japan (BSJ) 2011-11-18 /pmc/articles/PMC5036781/ /pubmed/27857599 http://dx.doi.org/10.2142/biophysics.7.113 Text en 2011 © The Biophysical Society of Japan This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Yoshidome, Takashi Importance of water entropy in rotation mechanism of F(1)-ATPase |
title | Importance of water entropy in rotation mechanism of F(1)-ATPase |
title_full | Importance of water entropy in rotation mechanism of F(1)-ATPase |
title_fullStr | Importance of water entropy in rotation mechanism of F(1)-ATPase |
title_full_unstemmed | Importance of water entropy in rotation mechanism of F(1)-ATPase |
title_short | Importance of water entropy in rotation mechanism of F(1)-ATPase |
title_sort | importance of water entropy in rotation mechanism of f(1)-atpase |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5036781/ https://www.ncbi.nlm.nih.gov/pubmed/27857599 http://dx.doi.org/10.2142/biophysics.7.113 |
work_keys_str_mv | AT yoshidometakashi importanceofwaterentropyinrotationmechanismoff1atpase |