Panfoli Isabella, Ponassi Marco, Ravera Silvia, Calzia Daniela, Beitia Maider, Morelli Alessandro, Rosano Camillo
Biochemistry Laboratory, Dept. of Pharmacy, University of Genova, Viale Benedetto XV, 3, 16132 Genova, Italy.
Proteomics Lab, IRCCS AOU San Martino - IST, National Institute for Cancer Research, Largo R. Benzi 10, 16132 Genova, Italy.
Biochem Biophys Res Commun. 2017 Jan 22;482(4):922-927. doi: 10.1016/j.bbrc.2016.11.134. Epub 2016 Nov 25.
FF-ATP synthase is a multisubunit enzyme responsible for the synthesis of ATP. Among its multiple subunits (8 in E. coli, 17 in yeast S. cerevisiae, 16 in vertebrates), two subunits a and c are known to play a central role controlling the H flow through the inner mitochondrial membrane which allows the subsequent synthesis of ATP, but the pathway followed by H within the two proteins is still a matter of debate. In fact, even though the structure of ATP synthase is now well defined, the molecular mechanisms determining the function of both F and F domains are still largely unknown. In this study, we propose a pathway for proton migration along the ATP synthase by hydrogen-bonded chain mechanism, with a key role of serine and threonine residues, by X-ray diffraction data on the subunit a of E. coli Fo.
