Hydride state intermediates are known to occur in various hydrogen conversion enzymes, including the highly efficient [FeFe] hydrogenases. The intermediate state involving a terminal iron-bound hydride has been recognized as crucial for the catalytic mechanism, but its occurrence has up to now eluded unequivocal proof under (near) physiological conditions. Here we show that the terminal hydride in the [FeFe] hydrogenase from Chlamydomonas reinhardtii can be directly detected using solution 1H NMR spectroscopy at room temperature, opening new avenues for detailed in situ investigations under catalytic conditions.

中文翻译：

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用核磁共振光谱法直接检测 [FeFe] 氢化酶中的末端氢化物中间体

已知氢化物中间体存在于各种氢转化酶中，包括高效的 [FeFe] 氢化酶。涉及末端铁键合氢化物的中间态已被认为对催化机制至关重要，但迄今为止，在（近）生理条件下，其发生尚无明确证据。在这里，我们表明可以在室温下使用溶液 1H NMR 光谱直接检测来自莱茵衣藻的 [FeFe] 氢化酶中的末端氢化物，为在催化条件下进行详细的原位研究开辟了新的途径。