title: Proton-linked L-fucose transport in Escherichia coli.
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.
authors.affiliation: Department of Biochemistry, University of Cambridge, U.K.
authors.forename: S A
authors.initials: SA
authors.lastname: Bradley
authors.forename: C R
authors.initials: CR
authors.lastname: Tinsley
authors.forename: J A
authors.initials: JA
authors.lastname: Muiry
authors.forename: P J
authors.initials: PJ
authors.lastname: Henderson
mesh_terms: D000963:Antimetabolites / Q000494:pharmacology; D001692:Biological Transport / Q000187:drug effects; D050260:Carbohydrate Metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D005643:Fucose / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011522:Protons; D013347:Subcellular Fractions / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000963:Antimetabolites; D011522:Protons; D005643:Fucose