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The c-Ring of the F1FO-ATP Synthase: Facts and Perspectives

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Abstract

The F1FO-ATP synthase is the only enzyme in nature endowed with bi-functional catalytic mechanism of synthesis and hydrolysis of ATP. The enzyme functions, not only confined to energy transduction, are tied to three intrinsic features of the annular arrangement of c subunits which constitutes the so-called c-ring, the core of the membrane-embedded FO domain: (i) the c-ring constitution is linked to the number of ions (H+ or Na+) channeled across the membrane during the dissipation of the transmembrane electrochemical gradient, which in turn determines the species-specific bioenergetic cost of ATP, the “molecular currency unit” of energy transfer in all living beings; (ii) the c-ring is increasingly involved in the mitochondrial permeability transition, an event linked to cell death and to most mitochondrial dysfunctions; (iii) the c subunit species-specific amino acid sequence and susceptibility to post-translational modifications can address antibacterial drug design according to the model of enzyme inhibitors which target the c subunits. Therefore, the simple c-ring structure not only allows the F1FO-ATP synthase to perform the two opposite tasks of molecular machine of cell life and death, but it also amplifies the enzyme’s potential role as a drug target.

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  1. Department of Veterinary Medical Sciences (DIMEVET), University of Bologna, Via Tolara di Sopra, 50, 40064, Ozzano Emilia, Bologna, Italy

    Salvatore Nesci, Fabiana Trombetti, Vittoria Ventrella & Alessandra Pagliarani

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  1. Salvatore Nesci
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Nesci, S., Trombetti, F., Ventrella, V. et al. The c-Ring of the F1FO-ATP Synthase: Facts and Perspectives. J Membrane Biol 249, 11–21 (2016). https://doi.org/10.1007/s00232-015-9860-3

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