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Originally published as Biophys J. BioFAST on April 13, 2007.
doi:10.1529/biophysj.107.109165
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Biophysical Journal 92:L103-L105 (2007)
© 2007 The Biophysical Society

On the Equivalence Point for Ammonium (De)protonation during Its Transport through the AmtB Channel

David L. Bostick and Charles L. Brooks, III

Department of Molecular Biology and Center for Theoretical Biological Physics, The Scripps Research Institute, La Jolla, California 92037

Correspondence: Address reprint requests and inquiries to Charles Brooks, E-mail: brooks{at}scripps.edu.

Structural characterization of the bacterial channel, AmtB, provides a glimpse of how members of its family might control the protonated state of permeant ammonium to allow for its selective passage across the membrane. In a recent study, we employed a combination of simulation techniques that suggested ammonium is deprotonated and reprotonated near dehydrative phenylalanine landmarks (F107 and F31, respectively) during its passage from the periplasm to the cytoplasm. At these landmarks, ammonium is forced to maintain a critical number (~3) of hydrogen bonds, suggesting that the channel controls ammonium (de)protonation by controlling its coordination/hydration. In the work presented here, a free energy-based analysis of ammonium hydration in dilute aqueous solution indicates, explicitly, that at biological pH, the transition from ammonium (Formula) to ammonia (NH3) occurs when these species are constrained to donate three hydrogen bonds or less. This result demonstrates the viability of the proposal that AmtB indirectly controls ammonium (de)protonation by directly controlling its hydration.




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