Metodiewa D, Marquez L A, Dunford H B
Department of Chemistry, University of Alberta, Edmonton, Canada.
Biochem Int. 1991 Jan;23(2):281-90.
Spectral evidence is presented which shows that butylated hydroxyanisole (BHA) and its dimer act as electron donors for lactoperoxidase (LPO) and myeloperoxidase (MPO) by two different pathways: peroxidative and oxidative. LPO compound II and MPO compound II are converted to native enzymes in their reactions with BHA without detectable intermediates. This confirms a normal peroxidatic oxidation of this commonly used antioxidant. We also report spectral data indicating the reductions of peroxidase compound III to the native state in reactions with BHA (LPO, MPO) or with di-BHA (LPO). This oxidative reaction has significant physiological relevance, ensuring return of peroxidases to the native state for re-entry into the normal peroxidatic cycle or into halogenating reactions.
有光谱证据表明，丁基羟基茴香醚（BHA）及其二聚体通过两种不同途径作为乳过氧化物酶（LPO）和髓过氧化物酶（MPO）的电子供体：过氧化途径和氧化途径。LPO化合物II和MPO化合物II在与BHA反应时转化为天然酶，且未检测到中间产物。这证实了这种常用抗氧化剂的正常过氧化氧化过程。我们还报告了光谱数据，表明在与BHA（LPO、MPO）或二 - BHA（LPO）反应时，过氧化物酶化合物III还原为天然状态。这种氧化反应具有重要的生理意义，可确保过氧化物酶恢复到天然状态，以便重新进入正常的过氧化循环或卤化反应。
