Lisov A V, Leont'evskiĭ A A, Golovleva L A
Prikl Biokhim Mikrobiol. 2007 Sep-Oct;43(5):598-606.
The Mn-peroxidase from the fungus Panus tigrinus 8/18 is a hybrid enzyme. It catalyzes both Mn2+-dependent and Mn2+-independent oxidation of organic substrates. The spectral properties of intermediates and the pathway of the catalytic cycle are typical of hybrid Mn-peroxidases. The enzyme catalyzes the "oxidase" reaction (NADH oxidation) without peroxide and with the presence of Mn2+, which takes part in hydrogen peroxide production via Mn3+ and preserves the enzyme from inactivation. With the presence of organic mediators, the hybrid Mn-peroxidase oxidizes nonphenolic compounds: aromatic alcohols and a nonphenolic lignin model compound. The degree of conversion of 2,4,6-trichlorophenol is higher with the presence of l-hydroxybenzotriazole.
来自真菌虎皮香菇8/18的锰过氧化物酶是一种杂合酶。它催化有机底物的锰离子依赖性和非锰离子依赖性氧化反应。中间体的光谱特性和催化循环途径是杂合锰过氧化物酶的典型特征。该酶在没有过氧化物且存在锰离子的情况下催化“氧化酶”反应(NADH氧化),锰离子通过锰(III)参与过氧化氢的产生,并保护酶不被失活。在有机介质存在的情况下,杂合锰过氧化物酶可氧化非酚类化合物:芳香醇和一种非酚类木质素模型化合物。在1-羟基苯并三唑存在的情况下,2,4,6-三氯苯酚的转化程度更高。