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PubMed Publications| Keyword search (4,163 papers available) |  |
"Lamoureux G" Authored Publications:
| Title | Authors | PubMed ID | |
|---|---|---|---|
| 1 | Ammonium transporters achieve charge transfer by fragmenting their substrate | Wang S; Orabi EA; Baday S; Bernèche S; Lamoureux G; | 22631217 CERMM |
| 2 | Identification of a cholesterol-binding pocket in inward rectifier K(+) (Kir) channels | Fürst O; Nichols CG; Lamoureux G; D' Avanzo N; | 25517146 CERMM |
| 3 | Salt-Dependent Interactions between the C-Terminal Domain of Osmoregulatory Transporter ProP of Escherichia coli and the Lipid Membrane | Ozturk TN; Culham DE; Tempelhagen L; Wood JM; Lamoureux G; | 32838524 CERMM |
| 4 | Genetic, Structural, and Functional Evidence Link TMEM175 to Synucleinopathies | Krohn L; Öztürk TN; Vanderperre B; Ouled Amar Bencheikh B; Ruskey JA; Laurent SB; Spiegelman D; Postuma RB; Arnulf I; Hu MTM; Dauvilliers Y; Högl B; Stefani A; Monaca CC; Plazzi G; Antelmi E; Ferini-Strambi L; Heidbreder A; Rudakou U; Cochen De Cock V; Young P; Wolf P; Oliva P; Zhang XK; Greenbaum L; Liong C; Gagnon JF; Desautels A; Hassin-Baer S; Montplaisir JY; Dupré N; Rouleau GA; Fon EA; Trempe JF; Lamoureux G; Alcalay RN; Gan-Or Z; | 31658403 CERMM |
| 5 | Drude polarizable force field for cation-π interactions of alkali and quaternary ammonium ions with aromatic amino acid side chains | Orabi EA; Davis RL; Lamoureux G; | 31652004 CERMM |
| 6 | Dual Role of the C-Terminal Domain in Osmosensing by Bacterial Osmolyte Transporter ProP | Culham DE; Marom D; Boutin R; Garner J; Ozturk TN; Sahtout N; Tempelhagen L; Lamoureux G; Wood JM; | 30448037 CHEMBIOCHEM |
| Title: | Ammonium transporters achieve charge transfer by fragmenting their substrate | ||||
| Authors: | Wang S, Orabi EA, Baday S, Bernèche S, Lamoureux G | ||||
| Link: | https://pubmed.ncbi.nlm.nih.gov/22631217/ | ||||
| DOI: | 10.1021/ja300129x | ||||
| Publication: | Journal of the American Chemical Society | ||||
| Keywords: | |||||
| PMID: | 22631217 | Category: | Date Added: | 2012-05-29 | |
| Dept Affiliation: |
CERMM
1 Department of Chemistry and Biochemistry and Centre for Research in Molecular Modeling (CERMM), Concordia University, 7141 Sherbrooke Street West, Montréal, Québec H4B?1R6, Canada. |
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Description: |
Proteins of the Amt/MEP family facilitate ammonium transport across the membranes of plants, fungi, and bacteria and are essential for growth in nitrogen-poor environments. Some are known to facilitate the diffusion of the neutral NH(3), while others, notably in plants, transport the positively charged NH(4)(+). On the basis of the structural data for AmtB from Escherichia coli , we illustrate the mechanism by which proteins from the Amt family can sustain electrogenic transport. Free energy calculations show that NH(4)(+) is stable in the AmtB pore, reaching a binding site from which it can spontaneously transfer a proton to a pore-lining histidine residue (His168). The substrate diffuses down the pore in the form of NH(3), while the excess proton is cotransported through a highly conserved hydrogen-bonded His168-His318 pair. This constitutes a novel permeation mechanism that confers to the histidine dyad an essential mechanistic role that was so far unknown. |
