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Heterobimetallic Models of the [NiFe] Hydrogenases: A Structural and Spectroscopic Comparison
Comments on Inorganic Chemistry ( IF 3.8 ) Pub Date : 2015-12-29 , DOI: 10.1080/02603594.2015.1108914
Shelby L. Behnke , Hannah S. Shafaat

Hydrogen has emerged as a leading alternative fuel; however, efficient chemical methods for generating hydrogen from water are lacking. Thus, chemists have turned to nature for inspiration. The [NiFe] hydrogenases possess rich structural, spectroscopic, and functional properties, motivating extensive synthetic efforts to model the complex active sites. In this comment, the geometric and electronic structures of the [NiFe] hydrogenases are compared to model compounds that most closely reproduce features of the native enzyme. The implications of this comparison and opportunities for advancing the catalytic activity of model compounds are discussed.



中文翻译:

[NiFe]氢化酶的异双金属模型:结构和光谱比较。

氢已成为主要的替代燃料。但是,缺乏从水中产生氢的有效化学方法。因此,化学家已经转向自然寻求灵感。[NiFe]氢化酶具有丰富的结构,光谱和功能特性,激发了广泛的合成努力来模拟复杂的活性位点。在此评论中,将[NiFe]氢化酶的几何和电子结构与最接近重现天然酶特征的模型化合物进行了比较。讨论了这种比较的含义以及提高模型化合物催化活性的机会。

更新日期:2015-12-29
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