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Crude extracts of Mycobacterium tuberculosis H37Ra, an isonicotinic acid hydrazide (isoniazid) (INH)-susceptible strain which has peroxidase activity, catalyzed the production of catechol from phenol in the presence of INH and H2O2 as shown by the development of the 444-nm absorption peak of oxidized catechol product. Extracts of the INH-resistant strain of M. tuberculosis H37Ra, which has no peroxidase, did not catalyze the reaction. The rate of development of the 444-nm peak increased proportionately with increased superoxide dismutase concentrations. The hydroxyl radical (. OH) scavengers dimethylsulfoxide and mannitol inhibited the reaction. Isonicotinamide, isonicotinic acid, and nicotinic acid could not replace INH.

Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra