PMID:15317788

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Citation

Grass, G, Thakali, K, Klebba, PE, Thieme, D, Müller, A, Wildner, GF and Rensing, C (2004) Linkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli. J. Bacteriol. 186:5826-33

Abstract

The multicopper oxidase CueO had previously been demonstrated to exhibit phenoloxidase activity and was implicated in intrinsic copper resistance in Escherichia coli. Catecholates can potentially reduce Cu(II) to the prooxidant Cu(I). In this report we provide evidence that CueO protects E. coli cells by oxidizing enterobactin, the catechol iron siderophore of E. coli, in the presence of copper. In vitro, a mixture of enterobactin and copper was toxic for E. coli cells, but the addition of purified CueO led to their survival. Deletion of fur resulted in copper hypersensitivity that was alleviated by additional deletion of entC, preventing synthesis of enterobactin. In addition, copper added together with 2,3-dihydroxybenzoic acid or enterobactin was able to induce a Phi(cueO-lacZ) operon fusion more efficiently than copper alone. The reaction product of the 2,3-dihydroxybenzoic acid oxidation by CueO that can complex Cu(II) ions was determined by gas chromatography-mass spectroscopy and identified as 2-carboxymuconate.

Links

PubMed PMC516812 Online version:10.1128/JB.186.17.5826-5833.2004

Keywords

Anti-Bacterial Agents/pharmacology; Artificial Gene Fusion; Bacterial Proteins/genetics; Bacterial Proteins/physiology; Copper/pharmacology; Drug Resistance, Bacterial/physiology; Enterobactin/metabolism; Enterobactin/pharmacology; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Gene Deletion; Gene Expression Regulation, Bacterial; Genes, Bacterial/genetics; Genes, Bacterial/physiology; Genes, Reporter; Hydroxybenzoates/metabolism; Oxidation-Reduction; Oxidoreductases/metabolism; Repressor Proteins/genetics; Repressor Proteins/physiology; Siderophores/metabolism; beta-Galactosidase/genetics; beta-Galactosidase/metabolism

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