New Perspective on the Reversibility of ATP Synthesis and Hydrolysis by Fo·F1-ATP Synthase (Hydrolase)

• Published in: Biochemistry (Moscow) Vol. 84; no. 11; pp. 1247 - 1255
• Main Author: Vinogradov, A. D.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01.11.2019; Springer Nature B.V
• Subjects: ATP; ATP synthase; Binding sites; Biochemistry; Bioenergetics; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Catalysis; Chemical synthesis; Chloroplasts; Coupling (molecular); Cytochrome; Dehydrogenases; Electrochemistry; Enzymes; Equilibrium; Free energy; Hydrogen ions; Hydrolase; Hydrolysis; Isoforms; Life Sciences; Membranes; Microbiology; Microorganisms; Mitochondria; Molecular machines; Phosphorylation; Physiology; Protonmotive force; Respiration; Review; reversibility of enzymatic catalysis; F; ATPase
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297919110038

F o ·F 1 -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 F o ·F 1 -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 F o ·F 1 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 F o ·F 1 unidirectionally catalyzing synthesis and/or hydrolysis of ATP.