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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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Autor principal: Yoshidome, Takashi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2011
Materias:
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.
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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
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