New Perspective on the Reversibility of ATP Synthesis and Hydrolysis by Fo·F1-ATP Synthase (Hydrolase)
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Fo·F1-ATPases of mitochondria, chloroplasts, and microorganisms catalyze transformation of proton motive force (the difference between the electrochemical potentials of hydrogen ion across a coupling membrane) to the free energy of ATP phosphoryl potential. It is often stated that Fo·F1-ATPases operate as reversible chemo-mechano-electrical molecular machines that provide either ATP synthesis or hydrolysis depending on particular physiological demands of an organism; the microreversibility principle of the enzyme catalysis is usually taken as a dogma. Since 1980, the author has upheld the view that the mechanisms of ATP synthesis and hydrolysis by the Fo·F1 complex are different (Vinogradov, A. D. (2000) J. Exp. Biol., 203, 41–49). In this paper, the author proposes a new model considering the existence in coupling membranes of two non-equilibrium isoforms of Fo·F1 unidirectionally catalyzing synthesis and/or hydrolysis of ATP.
KeywordsFo·F1-ATPase reversibility of enzymatic catalysis
H+-translocating ATPase (synthase)
proton motive force
inside-out Paracoccus denitrificans plasma membrane vesicles
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The author is grateful to his colleagues (all graduated from the Department of Biochemistry) who participated in the studies of Fo·F1. I thank Dr. V. G. Grivennikova for her great help in preparation of this manuscript and editorial comments.
This work has been continuously supported by the Russian Foundation for Basic Research, starting from its foundation (including current project 17-04-00706/17).
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