Hydrogen Bonding to a Dinitrogen Complex at Room Temperature: Impacts on N2 Activation.
Hydrogen Bonding to a Dinitrogen Complex at Room Temperature: Impacts on N2 Activation.
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DOI：
10.1021/jacs.9b02288
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发表时间：
2019-05
影响因子：
15
通讯作者：
J. P. Shanahan;N. Szymczak
中科院分区：
文献类型：
--
作者：
J. P. Shanahan;N. Szymczak
我们报告了一个实验和计算分析的影响氢键的金属二氮配合物。在室温下，一系列p Ka范围（Δ 20）内的H键供体与ReI-（N2）复合物的氮单元相互作用。通过~（15）N NMR、IR光谱、缔合平衡和密度泛函理论（DFT）研究表明，氢键相互作用使N-N键极化并减弱。这些结果提供了深入了解固氮酶的二级球残基的作用。
We report an experimental and computational analysis of the effects of hydrogen bonding to a metal dinitrogen complex. A series of H-bond donors over a wide p Ka range (Δ 20) interact with the nitrogen unit of a ReI-(N2) complex at room temperature. Analysis by 15N NMR, IR spectroscopy, association equilibria, and DFT studies indicates that the H-bonding interaction polarizes and weakens the N-N bond. These results provide insight into the role of the secondary sphere residues in nitrogenase enzymes.