Kinetic modelling of the proton translocating CF0CF1-ATP synthase from spinach.
The rate of both ATP synthase and hydrolysis catalysed by the thiol-modulated and activated ATP synthase from spinach is measured as a function of all substrates including the protons inside the thylakoid lumen. The most important findings are: (1) sigmoid kinetics with respect to H+in, (2) hyperbolic kinetics with respect to ADP, ATP and phosphate, with Km for phosphate and ADP decreasing upon increasing H+in, (3) binding of ADP and phosphate in random order and competitive to ATP. Simulation of the complete set of experimental data is obtained by a kinetic model featuring Boyer's binding-chain mechanism.
Pänke
O
O
Max-Volmer-Institut für Biophysikalische und Physikalische Chemie, Technische Universität, Berlin, Germany.
Rumberg
B
B
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D001667:Binding, Competitive; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D010710:Phosphates / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D018724:Spinacia oleracea / Q000201:enzymology*
D010710:Phosphates; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases