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The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate
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SYSNO ASEP 0475665 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title The lateral distance between a proton pump and ATP synthase determines the ATP-synthesis rate Author(s) Sjöholm, C. (SE)
Bergstrand, J. (SE)
Nilsson, T. (SE)
Šachl, Radek (UFCH-W) RID, ORCID
von Ballmoos, Ch. (CH)
Widengren, J. (SE)
Brzezinski, P. (SE)Article number 2926 Source Title Scientific Reports. - : Nature Publishing Group - ISSN 2045-2322
Roč. 7, č. 1 (2017)Number of pages 12 s. Language eng - English Country GB - United Kingdom Keywords biological energy-conversion ; cytochrome-c-oxidase ; membrane-surface ; rhodobacter-sphaeroides Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry Method of publishing Open access Institutional support UFCH-W - RVO:61388955 UT WOS 000402879200011 EID SCOPUS 85020432705 DOI 10.1038/s41598-017-02836-4 Annotation 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 congruent to 100 nm) or giant (d congruent to 10 mu m) 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 bo3 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 similar to 80 nm. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2018
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