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Biochemical and electron microscopic characterization of the F 1 F 0 ATP Synthase from the hyperthermophilic eubacterium Aquifex aeolicus
Author(s) -
Peng Guohong,
Bostina Mihnea,
Radermacher Michael,
Rais Isam,
Karas Michael,
Michel Hartmut
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.09.062
Subject(s) - aquifex aeolicus , eubacterium , atp synthase , protein subunit , crystallography , mass spectrometry , chemistry , biology , enzyme , biochemistry , escherichia coli , genetics , bacteria , gene , chromatography
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 α, β, γ, δ and ε 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 δ subunit.