ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry

Hoffmann, Jan; Sokolova, Lucie; Preiss, Laura; Hicks, David B.; Krulwich, Terry A.; Morgner, Nina; Wittig, Ilka; Schägger, Hermann; Meier, Thomas; Brutschy, Bernd

doi:10.1039/c0cp00733a

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ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry

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Preiss, Laura
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Meier, Thomas
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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引用

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

引用: https://hdl.handle.net/11858/00-001M-0000-0024-D6EC-E

要旨

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.