Journal
JOURNAL OF BACTERIOLOGY
Volume 186, Issue 17, Pages 5826-5833Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.17.5826-5833.2004
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Funding
- NIEHS NIH HHS [ES04940] Funding Source: Medline
- NIGMS NIH HHS [R01 GM053836, R01 GM053836-09] Funding Source: Medline
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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.
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