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.
|Number of pages||6|
|Journal||Berichte der bunsen-Gesellschaft-Physical chemistry chemical physics|
|Publication status||Published - 1988|
- Electron Microscopy
- Biophysical Chemistry