Resonance Raman Spectroscopy on [NiFe] Hydrogenase Provides Structural Insights into Catalytic Intermediates and Reactions
Resonance Raman Spectroscopy on [NiFe] Hydrogenase Provides Structural Insights into Catalytic Intermediates and Reactions
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DOI：
10.1021/ja505119q
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发表时间：
2014-07-16
影响因子：
15
通讯作者：
Zebger, Ingo
中科院分区：
文献类型：
--
作者：
Horch, Marius;Schoknecht, Janna;Zebger, Ingo
[NiFe]氢化酶催化氢的可逆裂解，因此，代表了用于研究和开发无排放能量转换过程的模型系统。通过监测单个催化中间体的光谱技术，可以获得有关潜在分子机制的有价值的信息。在这里，我们采用共振拉曼光谱，并将其扩展到整个双核活性位点的耐氧[NiFe]氢化酶通过探测的金属配体模式的Fe和，第一次，Ni离子。在理论方法的支持下，这种方法允许从活性位点监测H-转移，并揭示了迄今为止未知的催化循环的氢结合中间体的结构和电子构型的新见解，从而提供了有关催化中间体和生物氢活化反应的关键信息。
[NiFe] hydrogenases catalyze the reversible cleavage of hydrogen and, thus, represent model systems for the investigation and exploitation of emission-free energy conversion processes. Valuable information on the underlying molecular mechanisms can be obtained by spectroscopic techniques that monitor individual catalytic intermediates. Here, we employed resonance Raman spectroscopy and extended it to the entire binuclear active site of an oxygen-tolerant [NiFe] hydrogenase by probing the metal-ligand modes of both the Fe and, for the first time, the Ni ion. Supported by theoretical methods, this approach allowed for monitoring H-transfer from the active site and revealed novel insights into the so far unknown structure and electronic configuration of the hydrogen-binding intermediate of the catalytic cycle, thereby providing key information about catalytic intermediates and reactions of biological hydrogen activation.