But P G, Fomina V A, Murav'ev R A, Rogovin V V
Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 119991 Russia.
Izv Akad Nauk Ser Biol. 2003 May-Jun(3):261-5.
Peroxisomal myeloperoxidase plays a key role in synthesis of oxidants by neutrophilic leukocytes. This heme protein consists of two subunits connected by a disulfide bond. The enzyme uses H2O2 and Cl- for synthesis of HOCl--the major oxidant produced by neutrophils. Besides the chlorination reaction, myeloperoxidase exhibits some other properties depending on its oxidation state. The enzyme significantly affects synthesis of oxidants in the cells depending on the competing substrate concentrations and other factors. O2.- is also a physiological substrate of myeloperoxidase. Its reaction with the enzyme determines how the cells utilize O2.- for pathogen elimination. O2.- affects the chlorinating and peroxidase activities of myeloperoxidase. In addition, O2.- reacts with the enzyme yielding the catalytically active compound III that hydroxylates phenols.
过氧化物酶体髓过氧化物酶在嗜中性白细胞合成氧化剂的过程中起关键作用。这种血红素蛋白由通过二硫键连接的两个亚基组成。该酶利用过氧化氢和氯离子合成次氯酸——嗜中性白细胞产生的主要氧化剂。除了氯化反应外,髓过氧化物酶根据其氧化状态还表现出一些其他特性。该酶根据竞争性底物浓度和其他因素显著影响细胞内氧化剂的合成。超氧阴离子也是髓过氧化物酶的生理底物。它与该酶的反应决定了细胞如何利用超氧阴离子来消除病原体。超氧阴离子影响髓过氧化物酶的氯化和过氧化物酶活性。此外,超氧阴离子与该酶反应生成催化活性化合物III,该化合物可使酚羟基化。