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  ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry

Hoffmann, J., Sokolova, L., Preiss, L., Hicks, D. B., Krulwich, T. A., Morgner, N., et al. (2010). ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry. Physical Chemistry Chemical Physics, 12(41), 13375-13382. doi:10.1039/c0cp00733a.

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 Creators:
Hoffmann, Jan, Author
Sokolova, Lucie, Author
Preiss, Laura1, Author           
Hicks, David B., Author
Krulwich, Terry A., Author
Morgner, Nina, Author
Wittig, Ilka, Author
Schägger, Hermann, Author
Meier, Thomas1, Author           
Brutschy, Bernd, Author
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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 Abstract: Mass spectrometry of membrane protein complexes is still a methodological challenge due to hydrophobic and hydrophilic parts of the species and the fact that all subunits are bound non-covalently together. The present study with the novel laser induced liquid bead ion desorption mass spectrometry (LILBID-MS) reports on the determination of the subunit composition of the F(1)F(o)-ATP synthase from Bacillus pseudofirmus OF4, that of both bovine heart and, for the first time, of human heart mitochondrial F(1)F(o)-ATP synthases. Under selected buffer conditions the mass of the intact F(1)F(o)-ATP synthase of B. pseudofirmus OF4 could be measured, allowing the analysis of complex subunit stoichiometry. The agreement with theoretical masses derived from sequence databases is very good. A comparison of the ATP synthase subunit composition of 5 different ATPases reveals differences in the complexity of eukaryotic and bacterial ATP synthases. However, whereas the overall construction of eukaryotic enzymes is more complex than the bacterial ones, functionally important subunits are conserved among all ATPases.

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Language(s): eng - English
 Dates: 2010-11
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 517027
DOI: 10.1039/c0cp00733a
 Degree: -

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Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
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Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: - Volume / Issue: 12 (41) Sequence Number: - Start / End Page: 13375 - 13382 Identifier: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1