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Antimicrobial Agents and Chemotherapy, March 1998, p. 709-711, Vol. 42, No. 3
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Role of Superoxide in Catalase-Peroxidase-Mediated Isoniazid Action against Mycobacteria

Jian-Ying Wang,1 Richard M. Burger,1,2,* and Karl Drlica1

Public Health Research Institute, New York, New York 10016,1 and Redox Pharmaceutical Corporation, Greenvale, New York 115482

Received 19 September 1997/Returned for modification 12 December 1997/Accepted 29 December 1997

Isoniazid (INH) activation in vitro is associated with reduction of the mycobacterial ferric KatG catalase-peroxidase by hydrazine and reaction with O2 to form an oxyferrous enzyme complex. Since this complex could also form directly via reaction of ferric KatG with superoxide, intracellular activation might be responsive to superoxide concentration. When Mycobacterium smegmatis carrying the M. bovis katG gene was treated with nontoxic levels of plumbagin, a generator of superoxide, the bacteriostatic activity of INH increased unless a plasmid-borne superoxide dismutase gene was also present. Thus, endogenous superoxide probably contributes to intracellular activation of INH.

* Corresponding author. Mailing address: Public Health Research Institute, 455 First Ave., New York, NY 10016. Phone: (212) 576-8428. Fax: (212) 578-0804. E-mail: burger{at}phri.nyu.edu.

Antimicrobial Agents and Chemotherapy, March 1998, p. 709-711, Vol. 42, No. 3
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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  • Nguyen, M., Quemard, A., Broussy, S., Bernadou, J., Meunier, B. (2002). Mn(III) Pyrophosphate as an Efficient Tool for Studying the Mode of Action of Isoniazid on the InhA Protein of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 46: 2137-2144 [Abstract] [Full Text]  


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