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Volume 272, Number 14, Issue of April 4, 1997 pp. 8867-8870
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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COMMUNICATION:
The Role of Mn(II)-Peroxidase Activity of Mycobacterial Catalase-Peroxidase in Activation of the Antibiotic Isoniazid

(Received for publication, January 3, 1997, and in revised form, February 14, 1997)

From the Departments of Physiology and Biophysics and ^§ Biochemistry, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York 10461

The catalase-peroxidase of Mycobacteria smegmatis exhibits Mn(II)-peroxidase activity characterized by a low K_m for Mn(II) (5 µM) and a high K_m for t-butyl hydroperoxide (100 mM). This activity, monitored by the formation of Mn(III)-malate or -malonate, is inhibited by Co(II) but not by superoxide dismutase. Optical evidence for binding of Mn(II) to the resting (ferric) enzyme is found in a change in intensity of the Soret peak upon titration with Mn(II). A potential role for Mn(III) in the antimycobacterial action of the antibiotic isoniazid is suggested by the rapid reduction of Mn(III)-malonate by this drug. The stoichiometry of the reaction is consistent with two single electron transfer steps per mole of isoniazid.

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