The genetic identity and cofactor composition of the bacterial tellurate reductase are currently unknown. In this study, we examined the requirement of molybdopterin biosynthesis and molybdate transporter genes for tellurate reduction in Escherichia coli K-12. The results show that mutants deleted of the moaA, moaB, moaE, or mog gene in the molybdopterin biosynthesis pathway lost the ability to reduce tellurate. Deletion of the modB or modC gene in the molybdate transport pathway also resulted in complete loss of tellurate reduction activity. Genetic complementation by the wild-type sequences restored tellurate reduction activity in the mutant strains. These findings provide genetic evidence that tellurate reduction in E. coli involves a molybdoenzyme.T ellurium (Te) is a metalloid element used for a variety of industrial applications, including metallurgy, chemical manufacturing, electronics, and nanotechnology (1-4). The disposal of mine tailings and tellurium-containing waste has led to an increase in environmental contamination (5) . These oxyanions are highly toxic to microbiota (6) and cause inhibitory effects to most microorganisms at concentrations as low as 1 g/ml (1, 4). While naturally occurring Te-resistant bacteria have been isolated that are able to grow in the presence of elevated Te concentrations (7,8) and several genetic elements have been linked to Te resistance (9), the molecular mechanisms of bacterium-tellurium interactions remain poorly understood.Microorganisms are known to catalyze the reduction of toxic tellurite into sparingly soluble and less toxic elemental tellurium [Te(0)] (10-15). In comparison, little is known about the microbial reduction of tellurate, even though Te(VI) is the dominant form of Te in the hydrosphere (16,17). Recently, Shewanella species isolated from deep-ocean hydrothermal vent worms were discovered to respire Te(VI) as a terminal electron acceptor (18), and the anaerobic bacteria Sulfurospirillum barnesii and Bacillus selenitireducens were found to generate energy for growth on lactate by the reduction of Te(VI) to Te(0) (7). A Gram-positive bacterium, Bacillus beveridgei, was recently isolated that can also grow by reducing Te(VI) to Te(0) (8). The genetic identity and cofactor composition of enzymes that catalyze tellurate reduction in these bacteria, as well as other Te(VI) reducers, are currently unknown.The molybdenum cofactor forms the active site of several important bacterial redox proteins, including the enzymes that catalyze the reduction of selenium and arsenic (15,(19)(20)(21)(22)(23), two metalloid elements that share similar chemical characteristics with tellurium. In selenate [Se(VI)]-and arsenate [As(V)]-reducing bacteria, the assembly of the molybdoenzymes is dependent on molybdenum import into the cell and biosynthesis of the molybdopterin cofactor. Previous studies have demonstrated that molybdate uptake in Escherichia coli is facilitated by an ABC-type transporter, and the molybdopterin cofactor is constructed via a biosynthetic pathway enc...