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首页> 外文期刊>Polyhedron: The International Journal for Inorganic and Organometallic Chemistry >Extended Huckel calculations on functional and structural models of the FeMo-cofactor of nitrogenase
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Extended Huckel calculations on functional and structural models of the FeMo-cofactor of nitrogenase

机译：关于固氮酶FeMo辅因子功能和结构模型的扩展Huckel计算

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摘要

The possiblity of activating N_2 at the molybdenum centre of the FeMo-cofactor of nitrogenase is investigated using EHMO calculations on functional and structural models of the enzyme active site. We consider a diverse range of structurally defined complexes and elicit the EHMO characteristics of these sites. We then compare these with EHMO calculations on model clusters and FeMo-co with N_2 bound at Mo. Our focus is on both the binding of dinitrogen and its activation towards protonation. The latter requires a substantial occupation of the #pi#~* molecular orbitals of N_2 which is experimentally achieved in some mononuclear M-N_2 complexes. Binding and activation are also theoretically possible at the Mo centre of MoFe_3S_4 clusters provided they have the right oxidation state and geometry. However, structural deformations of the FeMo cofactor cluster core do not appear to provide a favourable situation for N_2-activation at Mo.
机译：在酶活性位点的功能和结构模型上，通过EHMO计算，研究了在固氮酶的FeMo辅因子的钼中心激活N_2的可能性。我们考虑了各种结构定义的复合物，并得出了这些位点的EHMO特征。然后，我们将这些与模型簇上的EHMO计算以及N_2结合在Mo上的FeMo-co进行比较。我们的重点是二氮的结合及其对质子化的激活。后者需要大量占据N_2的＃pi＃〜*分子轨道，这是在某些单核M-N_2配合物中通过实验实现的。理论上在MoFe_3S_4团簇的Mo中心也可以进行键合和活化，只要它们具有正确的氧化态和几何形状即可。然而，FeMo辅因子簇核心的结构变形似乎并未为Mo处的N_2活化提供有利条件。

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