Mycobacterium tuberculosis induces tuberculosis, which causes 3 million deaths annually throughout the world. Sulfur transport plays an important role in Mycobacterium tuberculosis. Thiosulfate sulfurtransferase (TST, EC: 2.8.1.1) is a limiting steps for the sulfur transfer reaction in the cellular, catalyzing the irreversible transfer of sulfane sulfur atom from a suitable donor. We engineered a genetic system to express high levels of recombinant Mycobacterium tuberculosis TST in Escherichia coli, treated the recombinant bacteria under sodium nitroprusside, and used this organism to test the role. Our studies show that conserved residues (Arg, Cys) of TST may be involved in the enzyme activity, and the role of the four thiosulfate sulfiirtransferases of MTB is may similar but not all the same. Under the drug of sodium nitroprusside, recombinant bacteria exhibit endurance. Moreover, we found not only cell viability depend upon expression of TST protein, but also depend upon existence of additive sodium thiosulfate. Then, a new mechanism was described to analyzing the relationship between thiosulfate sulfurtransferase of MTB and sodium nitroprusside. These results indicate that SseB play an important role in cyanide detoxification and Fe—S clusters. Sodium nitroprusside which has been traditionally used to treat high blood pressure may be a universal reagent.
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