AI Article Synopsis
- Many bacteria use siderophores to obtain iron, and the structure of these iron complexes influences how cells recognize and utilize them.
- Corynebactin, a siderophore from Gram-positive bacteria, is similar to enterobactin from Gram-negative bacteria but differs in its chemical structure.
- Research on the interactions and stability of ferric complexes shows that while enterobactin has one configuration, corynebactin has a Lambda configuration, and a hybrid version with serine produces a mix of structures with a slight preference for Lambda.
Article Abstract
Most species of bacteria employ siderophores to acquire iron. The chirality of the ferric siderophore complex plays an important role in cell recognition, uptake, and utilization. Corynebactin, isolated from Gram-positive bacteria, is structurally similar to enterobactin, a well known siderophore isolated from Gram-negative bacteria, but contains L-theronine instead of L-serine in the trilactone backbone. Corynebactin also contains a glycine spacer unit in each of the chelating arms. A hybrid analogue (serine-corynebactin) has been synthesized. The chirality and relative conformational stability of the three ferric complexes of enterobactin, corynebactin, and the hybrid has been investigated. In contrast to enterobactin, corynebactin assumes a Lambda configuration. However, the ferric serine-corynebactin hybrid forms a racemic mixture, only slightly favoring the Lambda conformation.
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