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Updated: Jul 19, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
Published on: January 22, 2019
Biochemical and electron microscopic characterization of the F1F0 ATP synthase from the hyperthermophilic eubacterium
Guohong Peng1, Mihnea Bostina, Michael Radermacher
1Max-Planck-Institut für Biophysik, Max-von-Laue-Str. 3, D-60438 Frankfurt am Main, Germany.
Abstract:
The F(1)F(0) ATP synthase has been purified from the hyperthermophilic eubacterium Aquifex aeolicus and characterized. Its subunits have been identified by MALDI-mass spectrometry through peptide mass fingerprinting and MS/MS. It contains the canonical subunits alpha, beta, gamma, delta and epsilon of F(1) and subunits a and c of F(0). Two versions of the b subunit were found, which show a low sequence homology to each other. Most likely they form a heterodimer. An electron microscopic single particle analysis revealed clear structural details, including two stalks connecting F(1) and F(0). In several orientations the central stalk appears to be tilted and/or kinked. It is unclear whether there is a direct connection between the peripheral stalk and the delta subunit.
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