Iron uptake and molecular recognition in Pseudomonas putida: Receptor mapping with ferrichrome and its biomimetic analogs

E. Jurkevitch, Y. Hadar*, Y. Chen, J. Libman, A. Shanzer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

The presence of an Fe3+-ferrichrome uptake system in fluorescent Pseudomonas spp. was demonstrated, and its structural requirements were mapped in Pseudomonas putida with the help of biomimetic ferrichrome analogs. Growth tests, 55Fe3+ uptake, and competition experiments demonstrated that the synthetic L-alanine derivative B5 inhibits the action of ferrichrome but does not facilitate Fe3+ transport, while the enantiomeric D-Ala derivative B6 fails to compete with ferrichrome. Contraction of the molecule's envelope by replacing L-Ala by glycine provided a synthetic carrier, B9, which fully simulates ferrichrome as a growth promoter. Sodium azide inhibited 55Fe3+ uptake of the Gly derivative B9, suggesting an active transport process. These data demonstrate the chiral discrimination of the ferrichrome receptor and its sensitivity to subtle structural changes. They further confirm that receptor binding is a necessary but not sufficient condition for Fe3+ uptake to occur and suggest that binding to the receptor and transport proteins might rely on different recognition patterns.

Original languageAmerican English
Pages (from-to)78-83
Number of pages6
JournalJournal of Bacteriology
Volume174
Issue number1
DOIs
StatePublished - 1992

Fingerprint

Dive into the research topics of 'Iron uptake and molecular recognition in Pseudomonas putida: Receptor mapping with ferrichrome and its biomimetic analogs'. Together they form a unique fingerprint.

Cite this