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Light-Driven Enzymatic Reaction in Thermophilic Protochlorophyllide Oxidoreductase

机译:嗜热偶氯化物氧化酶中的光驱动酶反应

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Within the chlorophyll biosynthetic pathway NADPH:protochlorophyllide oxidoreductase (POR; EC 1.3.1.33) catalyzes the light-dependent trans addition of hydrogen across the C17-C18 double bond of the D-ring of protochiorophyllide (Pchlide) to produce chlorophyllide (Chlide) (1). The fact that POR is light activated means the enzyme:substrate complex can be formed in the dark, removing the diffusive components out of the reaction. It was previously shown that the POR-catalyzed reaction can be observed in real time on a picosecond timescale after initiating catalysis with a 50 fs laser pulse. (2)In the present work. POR, from the thermophilic cyanobacterium The rmosvnechococcus elongatus BP-1, has been analyzed in the same way.
机译:在叶绿素生物合成途径NADPH:氧化氯化物氧化酶(POR; EC 1.3.1.33)催化在D11的D11-环(PCHLIDE)的C17-C18双键上氢的光依赖性反式添加氢气(PCHLIDE)中的C17-C18双键生产氯化物(克隆)( 1)。 POR是光激活的事实是指酶:酶:衬底复合物可以在黑暗中形成,从而从反应中除去漫射组分。之前表明,在用50 fs激光脉冲启动催化之后,可以实时观察到POR催化的反应。 (2)在目前的工作中。来自嗜热性蓝杆菌的POR,以相同的方式分析了RMOSVNECHOCCCUS Elongatus BP-1。

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