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Kinetic modelling of the proton translocating CF 0 CF 1 ‐ATP synthase from spinach
Author(s) -
Pänke Oliver,
Rumberg Bernd
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00246-3
Subject(s) - atp synthase , spinach , kinetics , atp hydrolysis , chemistry , chemiosmosis , phosphate , atp synthase gamma subunit , thylakoid , pi , biochemistry , enzyme , atpase , physics , chloroplast , quantum mechanics , gene
The rate of both ATP synthesis 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 K m 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‐change mechanism.