Peroxidase-mediated oxidation of isoniazid.
Oxidation of isonicotinic acid hydrazide (isoniazid) by horseradish peroxidase at the expense of H2O2 yielded reactive species which were able to reduce nitroblue tetrazolium and bleach p-nitrosodimethylaniline. Nicotinic acid hydrazide oxidation did not cause these effects. At slightly alkaline pH, oxidation of isonicotinic acid hydrazide by horseradish peroxidase proceeded at the expense of molecular O2, and the reaction was oxygen consuming. The addition of H2O2 abolished O2 consumption. Bovine liver catalase enhanced the rate of nitroblue tetrazolium reduction and decreased the maximal velocity of the reaction proportionately to catalase concentration. During oxidation of isonicotinic acid hydrazide by horseradish peroxidase-H2O2, splitting of the heme group of horseradish peroxidase took place as shown by the disappearance of the Soret and minor bands in the visible region of the spectrum.
D002374:Catalase / Q000494:pharmacology; D007538:Isoniazid / Q000378:metabolism*; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009580:Nitroblue Tetrazolium / Q000378:metabolism; D009603:Nitroso Compounds / Q000378:metabolism; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D010544:Peroxidases / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013997:Time Factors
D009603:Nitroso Compounds; C008651:4-nitrosodimethylaniline; D009580:Nitroblue Tetrazolium; D010544:Peroxidases; D002374:Catalase; D007538:Isoniazid