Exposure to the tellurium oxyanion tellurite (TeO3(2-)) results in the establishment of an oxidative stress status in most microorganisms. Usually, bacteria growing in the presence of the toxicant turn black because of the reduction of tellurite (Te(4+)) to the less-toxic elemental tellurium (Te(0)). In vitro, at least part of tellurite reduction occurs enzymatically in a nicotinamide dinucleotide-dependent reaction. In this work, we show that TeO3(2-) reduction by crude extracts of Escherichia coli overexpressing the zwf gene (encoding glucose-6-phosphate dehydrogenase) takes place preferentially in the presence of NADPH instead of NADH. The enzyme responsible for toxicant reduction was identified as 6-phosphogluconate dehydrogenase (Gnd). The gnd gene showed a subtle induction at short times after toxicant exposure while strains lacking gnd were more susceptible to the toxicant. These results suggest that both NADPH-generating enzymes from the pentose phosphate shunt may be involved in tellurite detoxification and resistance in E. coli.
Keywords: Escherichia coli; G6PDH; Gnd protein; NADPH; Tellurite reduction.
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