ATP Synthesis by Isolated Chloroplast Coupling Factors, Induced with pH-Shift
It is commonly accepted that the coupling of the energy-donating electron transfer in membranes of chloroplasts, mitochondria and bacteria with the energy-accepting reaction of ATP synthesis the major role belongs to the proton. This implies that at least some steps of the H+-ATPsynthase catalysed reaction are controlled by the deprotonation and protonation of several groups of the enzyme substrate complex (1,2). Therefore, it is quite natural that the attention of investigators is for more than 20 years attracted to the experiments of Jagendorf and Uribe (3), who revealed the ATP synthesis on the transfer of chloroplasts from acidic to alkaline media. We have attempted now to use this experimental approach to isolated protein coupling factors. The reaction of single-event ATP synthesis in solution, induced with acid-base shift, is treated as an “elementary act” which is multifold repeated with the alkaline shift in the suspension of thylakoid membranes. The protein which catalyses the direct (synthesis of ATP) and the reverse (hydrolysis) reactions occurs in the essentially different states.
KeywordsThylakoid Membrane Coupling Factor Enzyme Substrate Complex Alkaline Shift Conformational Relaxation
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