Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1.
Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1.
复制标题
假单胞菌甲苯/邻二甲苯单加氧酶羟化酶 T201S 变体中过氧二铁 (III) 中间体的表征。
DOI：
10.1021/ja9011782
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发表时间：
2009
影响因子：
15
通讯作者：
Lippard,StephenJ
中科院分区：
文献类型：
--
作者：
Song,WoonJu;Behan,RachelK;Naik,SunilG;Huynh,BoiHanh;Lippard,StephenJ
我们报告的观察一种新的中间体的反应中减少甲苯/邻二甲苯单加氧酶羟化酶（ToMOHred）T201 S的变体，在存在的调节蛋白（ToMOD），与分子氧。该物种是第一个在任何甲苯单加氧酶中具有光学带的含氧中间体。该中间体的紫外维斯和钼穆斯堡尔光谱特性使我们能够将其指定为过氧二铁（III）物种T201 Speroxo，类似于Hperoxoin甲烷单加氧酶。虽然T201 S产生T201 Speroxoin除了光学透明的ToMOHperoxo，以前观察到的野生型ToMOH，这种保守的变体是催化活性的稳态催化和单周转实验，并显示相同的区域特异性甲苯和略有不同的区域特异性邻二甲苯氧化。
We report the observation of a novel intermediate in the reaction of a reduced toluene/o-xylene monooxygenase hydroxylase (ToMOHred) T201S variant, in the presence of a regulatory protein (ToMOD), with dioxygen. This species is the first oxygenated intermediate with an optical band in any toluene monooxygenase. The UV−vis and Mössbauer spectroscopic properties of the intermediate allow us to assign it as a peroxodiiron(III) species, T201Speroxo, similar to Hperoxoin methane monooxygenase. Although T201S generates T201Speroxoin addition to optically transparent ToMOHperoxo, previously observed in wild-type ToMOH, this conservative variant is catalytically active in steady-state catalysis and single-turnover experiments and displays the same regiospecificity for toluene and slightly different regiospecificity foro-xylene oxidation.