The catalytic pathway of horseradish peroxidase at high resolution
The catalytic pathway of horseradish peroxidase at high resolution
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DOI：
10.1038/417463a
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发表时间：
2002-05-23
期刊：
影响因子：
64.8
通讯作者：
Hajdu, J
中科院分区：
文献类型：
--
作者：
Berglund, GI;Carlsson, GH;Hajdu, J
生物系统中氧和过氧化物活化的分子描述是困难的，因为在X射线数据收集期间释放的电子减少了催化这些反应的氧化还原酶的活性中心（1-5）。在这里，我们描述了一种有效的策略，以获得高化合价的氧化还原中间体的晶体结构，并提出了一个三维电影的X-射线驱动的催化还原辣根过氧化物酶（HRP）中的结合双氧物种。我们还描述了单独的实验，其中可以获得HRP所有五种氧化态的高分辨率结构，首次显示了保留氧化还原态的此类结构。
A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions(1-5). Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time.