In FoF1 (FoF1-ATP synthase), proton translocation through Fo drives rotation of the oligomer ring of Fo-c subunits (c-ring) relative to Fo-a. Previous reports have indicated that a conserved arginine residue in Fo-a plays a critical role in the proton transfer at the Fo-a/c-ring interface. Indeed, we show in the present study that thermophilic FoF1s with substitution of this arginine (aR169) to other residues cannot catalyse proton-coupled reactions. However, mutants with substitution of this arginine residue by a small (glycine, alanine, valine) or acidic (glutamate) residue mediate the passive proton translocation. This translocation requires an essential carboxy group of Fo-c (cE56) since the second mutation (cE56Q) blocks the translocation. Rotation of the c-ring is not necessary because the same arginine mutants of the ‘rotation-impossible’ (c10-a)FoF1, in which the c-ring and Fo-a are fused to a single polypeptide, also exhibits the passive proton translocation. The mutant (aR169G/Q217R), in which the arginine residue is transferred to putatively the same topological position in the Fo-a structure, can block the passive proton translocation. Thus the conserved arginine residue in Fo-a ensures proton-coupled c-ring rotation by preventing a futile proton shortcut.
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Research Article|
July 28 2010
Essential arginine residue of the Fo-a subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel
Noriyo Mitome
;
Noriyo Mitome
*
Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan
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Sakurako Ono
;
Sakurako Ono
*
Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan
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Hiroki Sato
;
Hiroki Sato
*
Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan
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Toshiharu Suzuki
;
Toshiharu Suzuki
†
ICORP, Japan Science and Technology Corporation (JST), 2-41 Aomi, Koto-ku, Tokyo 135-0064, Japan
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Nobuhito Sone
;
Nobuhito Sone
†
ICORP, Japan Science and Technology Corporation (JST), 2-41 Aomi, Koto-ku, Tokyo 135-0064, Japan
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Masasuke Yoshida
Masasuke Yoshida
1
*
Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan†
ICORP, Japan Science and Technology Corporation (JST), 2-41 Aomi, Koto-ku, Tokyo 135-0064, Japan‡
Department of Molecular Biosciences, Kyoto Sangyo University, Motoyama-Kamigamo, Kyoto 603-8555, Japan1
To whom correspondence should be addressed (email masasuke.yoshida@cc.kyoto-su.ac.jp).
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Biochem J (2010) 430 (1): 171-177.
Article history
Received:
April 22 2010
Revision Received:
May 24 2010
Accepted:
June 03 2010
Accepted Manuscript online:
June 03 2010
Citation
Noriyo Mitome, Sakurako Ono, Hiroki Sato, Toshiharu Suzuki, Nobuhito Sone, Masasuke Yoshida; Essential arginine residue of the Fo-a subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel. Biochem J 15 August 2010; 430 (1): 171–177. doi: https://doi.org/10.1042/BJ20100621
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