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. 1987 Dec 1;248(2):495–500. doi: 10.1042/bj2480495

Proton-linked L-fucose transport in Escherichia coli.

S A Bradley 1, C R Tinsley 1, J A Muiry 1, P J Henderson 1
PMCID: PMC1148569  PMID: 2829831

Abstract

1. Addition of L-fucose to energy-depleted anaerobic suspensions of Escherichia coli elicited an uncoupler-sensitive alkaline pH change diagnostic of L-fucose/H+ symport activity. 2. L-Galactose or D-arabinose were also substrates, but not inducers, for the L-fucose/H+ symporter. 3. L-Fucose transport into subcellular vesicles was dependent upon respiration, displayed a pH optimum of about 5.5, and was inhibited by protonophores and ionophores. 4. These results showed that L-fucose transport into E. coli was energized by the transmembrane electrochemical gradient of protons. 5. Neither steady state kinetic measurements nor assays of L-fucose binding to periplasmic proteins revealed the existence of a second L-fucose transport system.

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Selected References

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