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On the Equivalence Point for Ammonium (De)protonation During Its Transport Through the AmtB Channel

On the Equivalence Point for Ammonium (De)protonation During Its Transport Through the AmtB Channel

David L Bostick, Charles L Brooks 3rd

Biophys J. 2007 Jun 15;92(12):L103-5.

PMID: 17434945

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
ALP926023827	AMTB hydrate		926023-82-7 (anhydrous)	Price

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