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  On the Question of Hydronium Binding to ATP-Synthase Membrane Rotors

Leone, V., Krah, A., & Faraldo-Gómez, J. D. (2010). On the Question of Hydronium Binding to ATP-Synthase Membrane Rotors. Biophysical Journal, 99(7), L53-L55. doi:10.1016/j.bpj.2010.07.046.

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 Creators:
Leone, Vanessa1, Author           
Krah, Alexander1, Author           
Faraldo-Gómez, José D.1, Author           
Affiliations:
1Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068295              

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 Abstract: A recently determined atomic structure of an H(+)-coupled ATP-synthase membrane rotor has revived the long-standing question of whether protons may be bound to these structures in the form of a hydronium ion. Using both classical and quantum-mechanical simulations, we show that this notion is implausible. Ab initio molecular dynamics simulations of the binding site demonstrate that the putative H(3)O(+) deprotonates within femtoseconds. The bound proton is thus transferred irreversibly to the carboxylate side chain found in the ion-binding sites of all ATP-synthase rotors. This result is consistent with classical simulations of the rotor in a phospholipid membrane, on the 100-nanosecond timescale. These simulations show that the hydrogen-bond network seen in the crystal structure is incompatible with a bound hydronium. The observed coordination geometry is shown to correspond instead to a protonated carboxylate and a bound water molecule. In conclusion, this study underscores the notion that binding and transient storage of protons in the membrane rotors of ATP synthases occur through a common chemical mechanism, namely carboxylate protonation.

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Language(s): eng - English
 Dates: 2010-10
 Publication Status: Published in print
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 529546
DOI: 10.1016/j.bpj.2010.07.046
 Degree: -

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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 99 (7) Sequence Number: - Start / End Page: L53 - L55 Identifier: ISSN: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117