The rotary binding change mechanism of ATP synthases.
The F(0)F(1) ATP synthase functions as a rotary motor where subunit rotation driven by a current of protons flowing through F(0) drives the binding changes in F(1) that are required for net ATP synthesis. Recent work that has led to the identification of components of the rotor and stator is reviewed. In addition, a model is proposed to describe the transmission of energy from four proton transport steps to the synthesis of one ATP. Finally, some of the requirements for efficient energy coupling by a rotary binding change mechanism are considered.
Cross
R L
RL
Department of Biochemistry and Molecular Biology, State University of New York, Health Science Center, Syracuse, NY 13210, USA. crossr@hscsyr.edu
D025181:ATP Synthetase Complexes; D000255:Adenosine Triphosphate / Q000378:metabolism; D004734:Energy Metabolism; D008958:Models, Molecular; D020409:Molecular Motor Proteins; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011522:Protons
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