ArticleBiophysical journal2007
On the equivalence point for ammonium (de)protonation during its transport through the AmtB channel.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- A pore-occluding phenylalanine gate prevents ion slippage through plant ammonium transporters.Scientific reports · 2019Article
- The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Switching substrate specificity of AMT/MEP/ Rh proteins.Channels (Austin, Tex.) · 2014Review
- Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.Microbiology and molecular biology reviews : MMBR · 2013Review
- Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Periplasmic vestibule plays an important role for solute recruitment, selectivity, and gating in the Rh/Amt/MEP superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Statistical determinants of selective ionic complexation: ions in solvent, transport proteins, and other "hosts".Biophysical journal · 2009Article
- K+/Na+ selectivity in toy cation binding site models is determined by the 'host'.Biophysical journal · 2009Article
- Substrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Ammonia-induced formation of an AmtB-GlnK complex is not sufficient for nitrogenase regulation in the photosynthetic bacterium Rhodobacter capsulatus.Journal of bacteriology · 2008Article
- The 1.3-A resolution structure of Nitrosomonas europaea Rh50 and mechanistic implications for NH3 transport by Rhesus family proteins.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.