Shoeb H A, Bowman B U, Ottolenghi A C, Merola A J
Antimicrob Agents Chemother. 1985 Mar;27(3):399-403. doi: 10.1128/AAC.27.3.399.
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.
辣根过氧化物酶以过氧化氢为代价催化异烟肼（异烟酰肼）氧化产生的活性物质能够还原硝基蓝四氮唑并使对亚硝基二甲基苯胺褪色。烟酰肼氧化不会产生这些效应。在略碱性pH条件下，辣根过氧化物酶催化异烟肼氧化以分子氧为代价进行，该反应消耗氧气。加入过氧化氢可消除氧气消耗。牛肝过氧化氢酶提高了硝基蓝四氮唑的还原速率，并与过氧化氢酶浓度成比例地降低了反应的最大速度。在辣根过氧化物酶 - 过氧化氢催化异烟肼氧化过程中，辣根过氧化物酶的血红素基团发生裂解，这通过光谱可见区域中Soret带和小带的消失得以证明。
