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- W2028552201 abstract "TonB protein serves as an energy transducer to couple cytoplasmic membrane energy to high-affinity active transport of iron siderophores and vitamin B12 across the outer membranes of Gram-negative bacteria. The biochemical mechanism of the energy transduction remains to be determined, but important details are already known. TonB is targeted to and anchored in the cytoplasmic membrane by a single membrane-spanning domain and spans the periplasm to physically interact with outer-membrane receptors of the transport ligands. TonB-dependent energy transduction is modulated by ExbB protein, which stabilizes TonB, and possibly by several other proteins including ExbC, ExbD, and TolQ. TonB has a relatively short functional half-life that is accelerated when rates of active transport across the outer membrane are increased. A model that incorporates this information, as well as some tempered speculation, is presented." @default.
- W2028552201 created "2016-06-24" @default.
- W2028552201 creator A5055157480 @default.
- W2028552201 date "1990-12-01" @default.
- W2028552201 modified "2023-10-03" @default.
- W2028552201 title "TonB and the Gram-negative dilemma" @default.
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- W2028552201 doi "https://doi.org/10.1111/j.1365-2958.1990.tb00561.x" @default.
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