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Ammonium Transporters Achieve Charge Transfer by Fragmenting Their Substrate

Wang, Shihao, Orabi, Esam A., Baday, Sefer, Bernèche, Simon, Lamoureux, Guillaume
Journal of the American Chemical Society 2012 v.134 no.25 pp. 10419-10427
Escherichia coli, Gibbs free energy, ammonia, ammonium compounds, bacteria, binding sites, histidine, hydrogen bonding, plants (botany), transporters
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 NH₃, while others, notably in plants, transport the positively charged NH₄⁺. 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 NH₄⁺ 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 NH₃, 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.