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Updated: Aug 14, 2026

In vitro Investigation of the MexAB Efflux Pump From Pseudomonas aeruginosa
Published on: February 17, 2014
A new mechanism for membrane iron transport in Pseudomonas aeruginosa
I J Schalk1, M A Abdallah, F Pattus
1Département des Récepteurs et Protéines Membranaires UPR 9050 CNRS, ESBS, Bld Sébastien Brant, F-67400 Illkirch, Strasbourg, France. schalk@esbs.u-strasbg.fr
Abstract:
Various biochemical and biophysical studies have demonstrated the existence of a novel iron-uptake mechanism in Pseudomonas aeruginosa, different from that generally described for ferrichrome and ferric-enterobactin in Escherichia coli. This new iron-uptake mechanism involves all the proteins generally reported to be involved in the uptake of ferric-siderophore complexes in Gram-negative bacteria (i.e. the outer membrane receptor, periplasmic binding protein and ATP-binding-cassette transporter), but differs in the behaviour of the siderophore. One of the key features of this process is the binding of iron-free pyoverdin to the outer membrane receptor FpvA in conditions of iron deficiency.
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