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Stoichiometry of Energy Coupling by Proton-Translocating ATPases: A History of Variability

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Abstract

One of the central energy-coupling reactions in living systems is the intraconversion of ATP with a transmembrane proton gradient, carried out by proton-translocating F- and V-type ATPases/synthases. These reversible enzymes can hydrolyze ATP and pump protons, or can use the energy of a transmembrane proton gradient to synthesize ATP from ADP and inorganic phosphate. The stoichiometry of these processes (H+/ATP, or coupling ratio) has been studied in many systems for many years, with no universally agreed upon solution. Recent discoveries concerning the structure of the ATPases, their assembly and the stoichiometry of their numerous subunits, particularly the proton-carrying proteolipid (subunit c) of the FO and V0 sectors, have shed new light on this question and raise the possibility of variable coupling ratios modulated by variable proteolipid stoichiometries.

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  1. Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, 48201

    John J. Tomashek

  2. Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan, 48201

    William S. A. Brusilow

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Tomashek, J.J., Brusilow, W.S.A. Stoichiometry of Energy Coupling by Proton-Translocating ATPases: A History of Variability. J Bioenerg Biomembr 32, 493–500 (2000). https://doi.org/10.1023/A:1005617024904

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