Specific photoaffinity labelling of a ferripyoverdin outer membrane receptor of Pseudomonas aeruginosa

In order to identify and characterize the receptors involved in pyoverdin-mediated iron transport in Pseudomonas aeruginosa ATCC 15692, a photoactivatable siderophore has been synthesized. In the dark, this probe is stable and is able to promote iron transport at the same rate as the native pyoverdi...

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Bibliographic Details
Published in:FEBS letters 1996-11, Vol.396 (2), p.243-247
Main Authors: Ocaktan, Aydin, Schalk, Isabelle, Hennard, Christophe, Linget-Morice, Caroline, Kyslik, Pavel, Smith, Anthony W., Lambert, Peter A., Abdallah, Mohamed A.
Format: Article
Language:English
Subjects:
Affinity Labels
Affinity Labels - chemical synthesis
Affinity Labels - chemistry
Affinity Labels - metabolism
aminopyoverdin
Azides
Azides - chemical synthesis
Azides - chemistry
Azides - metabolism
Azidopyoverdin
Bacterial Outer Membrane Proteins
Bacterial Outer Membrane Proteins - analysis
Bacterial Outer Membrane Proteins - metabolism
Biochemistry, Molecular Biology
Electrophoresis, Polyacrylamide Gel
heteronuclear multiple bond correlation
heteronuclear multiple quantum coherence
HMBC
HMQC
HOHAHA
homonuclear Hartmann Hahn spectroscopy
Ion Transport
Iron
Iron - metabolism
Iron transport
Kinetics
Life Sciences
Oligopeptides
Outer membrane receptor
PaA
PaA-N3
PaA-NH2
Photoaffinity labelling
Pigments, Biological
Pigments, Biological - chemical synthesis
Pigments, Biological - chemistry
Pigments, Biological - metabolism
Pseudomonas aeruginosa
Pseudomonas aeruginosa - chemistry
Pseudomonas aeruginosa - metabolism
Pyoverdin
pyoverdin PaA
Siderophores
Siderophores - chemical synthesis
Siderophores - chemistry
Siderophores - metabolism
Ultraviolet Rays
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Summary:In order to identify and characterize the receptors involved in pyoverdin-mediated iron transport in Pseudomonas aeruginosa ATCC 15692, a photoactivatable siderophore has been synthesized. In the dark, this probe is stable and is able to promote iron transport at the same rate as the native pyoverdin. Under irradiation at 312 nm, the molecule is photodecomposed and a clear inhibition of the iron transport is observed. With the radioactive form of this photoactivatable probe, we were able to visualize on a SDS-PAGE gel a labelled protein of approximately 90 kDa molecular mass, which is very likely the FpvA receptor or a yet unknown pyoverdin receptor.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)01071-X