title: Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues.
abstract: F1Fo-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 F1and FOdomains 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.
authors.affiliation: Biochemistry Laboratory, Dept. of Pharmacy, University of Genova, Viale Benedetto XV, 3, 16132 Genova, Italy.
authors.forename: Isabella
authors.initials: I
authors.lastname: Panfoli
authors.affiliation: Proteomics Lab, IRCCS AOU San Martino - IST, National Institute for Cancer Research, Largo R. Benzi 10, 16132 Genova, Italy.
authors.forename: Marco
authors.initials: M
authors.lastname: Ponassi
authors.affiliation: Biochemistry Laboratory, Dept. of Pharmacy, University of Genova, Viale Benedetto XV, 3, 16132 Genova, Italy.
authors.forename: Silvia
authors.initials: S
authors.lastname: Ravera
authors.affiliation: Biochemistry Laboratory, Dept. of Pharmacy, University of Genova, Viale Benedetto XV, 3, 16132 Genova, Italy.
authors.forename: Daniela
authors.initials: D
authors.lastname: Calzia
authors.affiliation: Department of Nursing I, Medicine and Nursing Faculty, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain; Department of Physiology, Medicine and Nursing Faculty, University of the Basque Country (UPV/EHU), Leioa, Bizkaia, Spain; BioCruces Research Institute, Barakaldo, Bizkaia, Spain.
authors.forename: Maider
authors.initials: M
authors.lastname: Beitia
authors.affiliation: Biochemistry Laboratory, Dept. of Pharmacy, University of Genova, Viale Benedetto XV, 3, 16132 Genova, Italy.
authors.forename: Alessandro
authors.initials: A
authors.lastname: Morelli
authors.affiliation: Proteomics Lab, IRCCS AOU San Martino - IST, National Institute for Cancer Research, Largo R. Benzi 10, 16132 Genova, Italy. Electronic address: camillo.rosano@gmail.com.
authors.forename: Camillo
authors.initials: C
authors.lastname: Rosano
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011522:Protons; D016415:Sequence Alignment; D012694:Serine / Q000737:chemistry / Q000378:metabolism*; D013912:Threonine / Q000737:chemistry / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D029968:Escherichia coli Proteins; D011522:Protons; D013912:Threonine; D012694:Serine; D000255:Adenosine Triphosphate; C523987:ATP synthase subunit c, E coli; D025243:Bacterial Proton-Translocating ATPases; C074428:atpB protein, E coli
keywords: ATP synthase; Bioenergetics; Mitochondria; Molecular modelling; Proton wires