On the equivalence point for ammonium (de)protonation during its transport through the AmtB channel.
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 ( approximately 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 (NH(4)(+)) to ammonia (NH(3)) 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.
Bostick
David L
DL
Department of Molecular Biology and Center for Theoretical Biological Physics, The Scripps Research Institute, La Jolla, California 92037, USA.
Brooks
Charles L
CL
D027682:Cation Transport Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D003198:Computer Simulation; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D006860:Hydrogen Bonding; D015640:Ion Channel Gating; D017136:Ion Transport; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D011522:Protons; D000644:Quaternary Ammonium Compounds / Q000737:chemistry*; D014867:Water / Q000737:chemistry
C111096:AmtB protein, E coli; D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; D011522:Protons; D000644:Quaternary Ammonium Compounds; D014867:Water