On the Structure of the ATP-Synthase from Chloroplasts

Egbert J. Boekema, Petra Fromme, Peter Gräber

Research output: Contribution to journalArticleAcademic

Abstract

The H+-translocating ATPase ("ATP-synthase, CF0F1) was isolated from chloroplasts and characterized biochemically and by high resolution electron microscopy. The ATP-synthase has a hydrophilic part, CF1, and a hydrophobic part, CF0, with subunit composition I, II, III12, IV. The top view projection of CF1 (i.e. vertical to the membrane) reveals a pseudohexagonal arrangement of the large subunits α3β3, which are arranged in two layers. The α- and β-subunits are connected by a stalk with the membrane-integrated CF0 part. The shape and dimensions of CF0F1 are given and a model for the subunit arrangement is described.
Original languageEnglish
Pages (from-to)1031-1036
Number of pages6
JournalBerichte der bunsen-Gesellschaft-Physical chemistry chemical physics
Volume92
Publication statusPublished - 1988

Keywords

  • Membranes
  • Electron Microscopy
  • Catalysis
  • Biophysical Chemistry

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