The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate

Abstract We have investigated the effect of lipid composition on interactions between cytochrome bo 3 and ATP-synthase, and the ATP-synthesis activity driven by proton pumping. The two proteins were labeled by fluorescent probes and co-reconstituted in large (d ≅ 100 nm) or giant (d ≅ 10 µm) unilame...

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Autores principales:	Johannes Sjöholm, Jan Bergstrand, Tobias Nilsson, Radek Šachl, Christoph von Ballmoos, Jerker Widengren, Peter Brzezinski
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/854e6b1f99234dfd8912dff107157590
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spelling	oai:doaj.org-article:854e6b1f99234dfd8912dff1071575902021-12-02T11:40:13ZThe lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate10.1038/s41598-017-02836-42045-2322https://doaj.org/article/854e6b1f99234dfd8912dff1071575902017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02836-4https://doaj.org/toc/2045-2322Abstract We have investigated the effect of lipid composition on interactions between cytochrome bo 3 and ATP-synthase, and the ATP-synthesis activity driven by proton pumping. The two proteins were labeled by fluorescent probes and co-reconstituted in large (d ≅ 100 nm) or giant (d ≅ 10 µm) unilamellar lipid vesicles. Interactions were investigated using fluorescence correlation/cross-correlation spectroscopy and the activity was determined by measuring ATP production, driven by electron-proton transfer, as a function of time. We found that conditions that promoted direct interactions between the two proteins in the membrane (higher fraction DOPC lipids or labeling by hydrophobic molecules) correlated with an increased activity. These data indicate that the ATP-synthesis rate increases with decreasing distance between cytochrome bo 3 and the ATP-synthase, and involves proton transfer along the membrane surface. The maximum distance for lateral proton transfer along the surface was found to be ~80 nm.Johannes SjöholmJan BergstrandTobias NilssonRadek ŠachlChristoph von BallmoosJerker WidengrenPeter BrzezinskiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Johannes Sjöholm Jan Bergstrand Tobias Nilsson Radek Šachl Christoph von Ballmoos Jerker Widengren Peter Brzezinski The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
description	Abstract We have investigated the effect of lipid composition on interactions between cytochrome bo 3 and ATP-synthase, and the ATP-synthesis activity driven by proton pumping. The two proteins were labeled by fluorescent probes and co-reconstituted in large (d ≅ 100 nm) or giant (d ≅ 10 µm) unilamellar lipid vesicles. Interactions were investigated using fluorescence correlation/cross-correlation spectroscopy and the activity was determined by measuring ATP production, driven by electron-proton transfer, as a function of time. We found that conditions that promoted direct interactions between the two proteins in the membrane (higher fraction DOPC lipids or labeling by hydrophobic molecules) correlated with an increased activity. These data indicate that the ATP-synthesis rate increases with decreasing distance between cytochrome bo 3 and the ATP-synthase, and involves proton transfer along the membrane surface. The maximum distance for lateral proton transfer along the surface was found to be ~80 nm.
format	article
author	Johannes Sjöholm Jan Bergstrand Tobias Nilsson Radek Šachl Christoph von Ballmoos Jerker Widengren Peter Brzezinski
author_facet	Johannes Sjöholm Jan Bergstrand Tobias Nilsson Radek Šachl Christoph von Ballmoos Jerker Widengren Peter Brzezinski
author_sort	Johannes Sjöholm
title	The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
title_short	The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
title_full	The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
title_fullStr	The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
title_full_unstemmed	The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
title_sort	lateral distance between a proton pump and atp synthase determines the atp-synthesis rate
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/854e6b1f99234dfd8912dff107157590
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The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate

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