Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues
- 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)
- Department of Nursing I, Medicine and Nursing Faculty, University of the Basque Country (UPV/EHU), Leioa, Bizkaia (Spain)
F{sub 1}F{sub o}-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{sup +} flow through the inner mitochondrial membrane which allows the subsequent synthesis of ATP, but the pathway followed by H{sup +} 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{sub 1} and F{sub O} 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.
- OSTI ID:
- 22696788
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 482, Issue 4; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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