Structural Characterization of the Heterobactin Siderophores from Rhodococcus erythropolis PR4 and Elucidation of Their Biosynthetic Machinery

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• 作者：Mattia Bosello ; Mustafa Zeyadi ; Femke I. Kraas ; Uwe Linne ; Xiulan Xie ; Mohamed A. Marahiel
• 刊名：Journal of Natural Products
• 出版年：2013
• 出版时间：December 27, 2013
• 年：2013
• 卷：76
• 期：12
• 页码：2282-2290
• 全文大小：428K
• ISSN：1520-6025

文摘

In this study, the isolation, the structural characterization, and the elucidation of the biosynthetic origin of heterobactins, catecholate-hydroxamate mixed-type siderophores from Rhodococcus erythropolis PR4, are reported. The structure elucidation of heterobactin A was accomplished via MSⁿ analysis and NMR spectroscopy and revealed the noteworthy presence of a peptide bond between the guanidine group of an arginine residue and a 2,3-dihydroxybenzoate moiety. The two heterobactin S1 and S2 variants are derivatives of heterobactin A that have sulfonation modifications on the aromatic rings. The bioinformatic analysis of the R. erythropolis PR4 genome and the subsequent genetic and biochemical characterization of the putative biosynthetic machinery identified the gene cluster responsible for the biosynthesis of the heterobactins. Interestingly, the HtbG NRPS presents an unprecedented C-PCP-A domain organization within the second module of the synthetase that may help the correct elongation of the peptide intermediate. Finally, the present work revises the structure of heterobactin A that was described by Carrano et al. in 2001.