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Indole, a derivative of the amino acid tryptophan, is a toxic signaling molecule, which can inhibit bacterial growth. To overcome indole-induced toxicity, many bacteria have developed enzymatic defense systems to convert indole to non-toxic, water-insoluble indigo. We previously demonstrated that, like other aromatic compound-degrading bacteria,  Acinetobacter baumannii  can also convert indole to indigo. However, no work has been published investigating this mechanism. Here, we have shown that the growth of wild-type  A .  baumannii  is severely inhibited in the presence of 3.5 mM indole. However, at lower concentrations, growth is stable, implying that the bacteria may be utilizing a survival mechanism to oxidize indole. To this end, we have identified a flavoprotein oxygenase encoded by the  iifC  gene of  A .  baumannii . Further, our results suggest that expressing this recombinant oxygenase protein in  Escherichia coli  can drive indole oxidation to indigo  in vitro . Genome analysis shows that the  iif  operon is exclusively present in the genomes of  A .  baumannii  and  Pseudomonas syringae  pv.  actinidiae . Quantitative PCR and Western blot analysis also indicate that the  iif  operon is activated by indole through the AraC-like transcriptional regulator IifR. Taken together, these data suggest that this species of bacteria utilizes a novel indole-detoxification mechanism that is modulated by IifC, a protein that appears to be, at least to some extent, regulated by IifR.

Detoxification of Indole by an Indole-Induced Flavoprotein Oxygenase from Acinetobacter baumannii