title: Important subunit interactions in the chloroplast ATP synthase.
abstract: General structural features of the chloroplast ATP synthase are summarized highlighting differences between the chloroplast enzyme and other ATP synthases. Much of the review is focused on the important interactions between the epsilon and gamma subunits of the chloroplast coupling factor 1 (CF(1)) which are involved in regulating the ATP hydrolytic activity of the enzyme and also in transferring energy from the membrane segment, chloroplast coupling factor 0 (CF(0)), to the catalytic sites on CF(1). A simple model is presented which summarizes properties of three known states of activation of the membrane-bound form of CF(1). The three states can be explained in terms of three different bound conformational states of the epsilon subunit. One of the three states, the fully active state, is only found in the membrane-bound form of CF(1). The lack of this state in the isolated form of CF(1), together with the confirmed presence of permanent asymmetry among the alpha, beta and gamma subunits of isolated CF(1), indicate that ATP hydrolysis by isolated CF(1) may involve only two of the three potential catalytic sites on the enzyme. Thus isolated CF(1) may be different from other F(1) enzymes in that it only operates on 'two cylinders' whereby the gamma subunit does not rotate through a full 360 degrees during the catalytic cycle. On the membrane in the presence of a light-induced proton gradient the enzyme assumes a conformation which may involve all three catalytic sites and a full 360 degrees rotation of gamma during catalysis.
authors.affiliation: Department of Molecular Biosciences, The University of Kansas, Lawrence 66045, USA.
authors.forename: M L
authors.initials: ML
authors.lastname: Richter
authors.forename: R
authors.initials: R
authors.lastname: Hein
authors.forename: B
authors.initials: B
authors.lastname: Huchzermeyer
mesh_terms: D025181:ATP Synthetase Complexes; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D002736:Chloroplasts / Q000201:enzymology*; D005453:Fluorescence; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry; D009097:Multienzyme Complexes / Q000737:chemistry; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000737:chemistry; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D011522:Protons
chemical_list: D020409:Molecular Motor Proteins; D009097:Multienzyme Complexes; D011522:Protons; D000255:Adenosine Triphosphate; D025181:ATP Synthetase Complexes; D017856:Phosphotransferases (Phosphate Group Acceptor); D006180:Proton-Translocating ATPases