D. Research Applications:

2. Recognition on a Chiral Complex in the Mediated Transport of Iron by E. Coli
Research by K. Raymond (University of California Berkeley) and W. Rastetter (MIT)
b. Contrasting the Biological Activity of [&Delta -Iron(III)enterobactin]3- and [&Lambda -Iron(III)enantio-enterobactin]3-


This is the Proposed Structure of [&Delta-Iron(III)enterobactin]3-
based on the crystal structure of [&Delta-Vanadium(IV)enterobactin]2-
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Enterobactin is biosynthesized by E. Coli. Enterobactin binds to iron to form only the [&Delta -Iron(III)enterobactin]3- complex which is then transported into the organism at the ferric enterobactin protein (fep) receptor to supply iron (an essential element for life).
This is the Proposed Structure for [&Lambda -Iron(III)enantio-enterobactin]3- synthesized by W. Rastetter and his research collegues at MIT.
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[&Lambda -Iron(III)enantio-enterobactin]3- does not support growth in E. coli confirming that the recognition is stereospecific.
Reference: Rastetter, W.H., Erickson, T.J., Venuti, M. C.; The Journal of Organic Chemistry, Vol 46, 1981, p. 3579-3590. DOI

These observations confirmed that recognition by the fep protein receptor was stereospecific, however the question remained as to whether recognition took place on the tri-L-serine backbone or elsewhere in the molecule. Raymond's group established that recognition (surprisingly) occurred on the metal tris chelate region of the molecule.

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