Superoxide Reactivity of KatG: Insights into Isoniazid Resistance Pathways in TB

Journal of the American Chemical Society

Volumn 126, Issue 15, 2004, Pages 4772-4773

  Ghiladi, Reza A ^a   Cabelli, Diane E ^a   Ortiz De Montellano, Paul R ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; ISONIAZID; KATG PROTEIN; PEROXIDASE; SUPEROXIDE; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; HYDROGEN BOND; MINIMUM INHIBITORY CONCENTRATION; MULTIDRUG RESISTANCE; PULSE RADIOLYSIS; TUBERCULOSIS;

ANTITUBERCULAR AGENTS; BACTERIAL PROTEINS; CATALASE; DRUG RESISTANCE, BACTERIAL; ISONIAZID; MYCOBACTERIUM TUBERCULOSIS; OXIDOREDUCTASES; POINT MUTATION; PULSE RADIOLYSIS; SUPEROXIDES;

EID: 1842830219     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja031728t     Document Type: Article

References (20)

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16. HPLC was performed using an Alltech Nucleosil (C18) column (4.6 x 250 mm, 100 Å, 10 mm) employing a linear gradient from 0 to 37.5% (v/v) acetonitrile in 70 mM sodium acetate (pH 4.5) buffer. Products were monitored at 260 and 328 nm, and initial velocities were determined from integration of the peaks identified as INH-NADH adducts (A328/A260 = 3.3-3.55).
17. 2 binding, 5 or (ii) trace metals have been previously shown to catalyze the autoxidation of INH (or hydrazines in general), yielding superoxide.
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20. We would like to thank a reviewer for bringing this to our attention.