Iron uptake and molecular recognition in Pseudomonas putida: receptor mapping with ferrichrome and its biomimetic analogs.
The presence of an Fe(3+)-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.
Jurkevitch
E
E
Department of Microbiology and Plant Pathology, Faculty of Agriculture, Hebrew University of Jerusalem, Rehovot, Israel.
Hadar
Y
Y
Chen
Y
Y
Libman
J
J
Shanzer
A
A
D001425:Bacterial Outer Membrane Proteins; D001692:Biological Transport; D005290:Ferric Compounds / Q000378:metabolism; D005291:Ferrichrome / Q000031:analogs & derivatives / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D007504:Iron Radioisotopes / Q000378:metabolism; D016958:Pseudomonas putida / Q000235:genetics / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D005290:Ferric Compounds; D007504:Iron Radioisotopes; D011956:Receptors, Cell Surface; C035902:siderophore receptors; D005291:Ferrichrome; D007501:Iron