Journal of Bioenergetics and Biomembranes

, Volume 24, Issue 5, pp 441–445 | Cite as

The αβ complexes of ATP synthase: the α3β3 oligomer and α1β1 protomer

  • Yasuo Kagawa
  • Shigeo Ohta
  • Mitsuo Harada
  • Hiroshi Kihara
  • Yuji Ito
  • Mamoru Sato
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Abstract

The basic structures of the catalytic portion (F1, α3β3γδε) of ATP synthase are the α3β3 hexamer (oligomer with cooperativity) and α1β1 heterodimer (protomer). These were reconstituted from the α and β subunits of thermophilic F1 (TF1), and the α3β3 hexamer was crystallized. On electrophoresis, both the dimer and hexamer showed bands with ATPase activity. Using the dimer and hexamer, we studied the nucleotide-dependent rapid molecular dynamics. The formation of the hexamer required neither nucleotide nor Mg. The hexamer was dissociated into the dimer in the presence of MgADP, while the dimer was associated into the hexamer in the presence of MgATP. The hexamer, like mitochondrial F1 and TF1, showed two kinds of ATPase activity: one was cooperative and was inhibited by only one BzADP per hexamer, and the other was inhibited by three BzADP per hexamer.

Key words

ATP synthase F1 oligomer protomer molecular dynamics 
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Copyright information

© Plenum Publishing Corporation 1992

Authors and Affiliations

  • Yasuo Kagawa
    • 1
  • Shigeo Ohta
    • 1
  • Mitsuo Harada
    • 2
  • Hiroshi Kihara
    • 3
  • Yuji Ito
    • 4
  • Mamoru Sato
    • 5
  1. 1.Department of BiochemistryJichi Medical SchoolTochigiJapan
  2. 2.Department of PhysicsJichi Medical SchoolTochigiJapan
  3. 3.Department of NursingJichi Medical SchoolTochigiJapan
  4. 4.Institute for Solid State PhysicsThe University of TokyoTokyoJapan
  5. 5.Institute for Protein ResearchSuitaJapan

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