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Ferric iron uptake in Erwinia chrysanthemi mediated by chrysobactin and related catechol-type compounds.

Department of Molecular and Cell Biology, University of California, Berkeley 94720.

ABSTRACT

Erwinia chrysanthemi 3937 possesses a saturable, high-affinity transport system for the ferric complex of its native siderophore chrysobactin, [N-alpha-(2,3-dihydroxybenzoyl)-D-lysyl-L-serine]. Uptake of 55Fe-labeled chrysobactin was completely inhibited by respiratory poison or low temperature and was significantly reduced in rich medium. The kinetics of chrysobactin-mediated iron transport were determined to have apparent Km and Vmax values of about 30 nM and of 90 pmol/mg.min, respectively. Isomers of chrysobactin and analogs with progressively shorter side chains mediated ferric iron transport as efficiently as the native siderophore, which indicates that the chrysobactin receptor primarily recognizes the catechol-iron center. Free ligand in excess only moderately reduced the accumulation of 55Fe. Chrysobactin may therefore be regarded as a true siderophore for E. chrysanthemi.

This article has been cited by other articles:

• Rauscher, L., Expert, D., Matzanke, B. F., Trautwein, A. X. (2002). Chrysobactin-dependent Iron Acquisition in Erwinia chrysanthemi. FUNCTIONAL STUDY OF A HOMOLOG OF THE ESCHERICHIA COLI FERRIC ENTEROBACTIN ESTERASE. J. Biol. Chem. 277: 2385-2395 [Abstract] [Full Text]