Quaternary structure of ATP synthases: Symmetry and asymmetry in the F1 moiety L. Mario AmzelMario A. BianchetPeter L. Pedersen Minireview Pages: 429 - 433
Structure of theEscherichia coli ATP synthase and role of the γ and ε subunits in coupling catalytic site and proton channeling functions Roderick A. CapaldiRobert AggelerStephan Wilkens Minireview Pages: 435 - 439
The αβ complexes of ATP synthase: the α3β3 oligomer and α1β1 protomer Yasuo KagawaShigeo OhtaMamoru Sato Minireview Pages: 441 - 445
Identification of subunits required for the catalytic activity of the F1-ATPase Zippora Gromet-Elhanan Minireview Pages: 447 - 452
A model for the catalytic site of F1-ATPase based on analogies to nucleotide-binding domains of known structure Thomas M. DuncanRichard L. Cross Minireview Pages: 453 - 461
A glycine-rich sequence in the catalytic site of F-type ATPase Masamitsu FutaiAtsuko IwamotoMasatomo Maeda Minireview Pages: 463 - 467
Functional sites in F1-ATPases: Location and interactions William S. AllisonJean-Michel JaultSeung R. Paik Minireview Pages: 469 - 477
H+ transport and coupling by the F0 sector of the ATP synthase: Insights into the molecular mechanism of function Robert H. Fillingame Minireview Pages: 485 - 491
Proton transport-coupled unisite catalysis by the H+-ATPase from chloroplasts Peter GräberAndreas Labahn Minireview Pages: 493 - 497
Kinetic studies of ATP synthase: The case for the positional change mechanism Kathryn F. LaNoueJerzy Duszynski Minireview Pages: 499 - 506
Interaction of beef-heart mitochondrial F1-ATPase with immobilized ATP in the presence of dimethylsulfoxide Seelochan BeharryPhilip D. Bragg Original Article Pages: 507 - 514
