A Major Structural Change of the Homocitrate Ligand of Probable Importance for the Nitrogenase Mechanism,Inorganic Chemistry

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A Major Structural Change of the Homocitrate Ligand of Probable Importance for the Nitrogenase Mechanism
Inorganic Chemistry ( IF 4.3 ) Pub Date : 2018-01-05 00:00:00 , DOI: 10.1021/acs.inorgchem.7b02493
Per E. M. Siegbahn ₁

Affiliation

Mo-containing nitrogenase is the main enzyme that is able to take N₂ from the air and form ammonia. The active-site cofactor of the enzyme, termed FeMoco, is unique in nature. It has seven Fe and one Mo atoms connected by S bridges, with a C atom in the center of the cofactor. Another unusual feature is that it has a large homocitrate ligand known to be of importance for catalysis. In the present computational study, the role of the homocitrate ligand is investigated. It is found that a large structural change, which makes Mo^III five-coordinated, is energetically favorable in the more reduced states. This is of probable importance for the nitrogenase mechanism.

中文翻译：

硝化酶机制可能重要的同质配体的主要结构变化

含钼的固氮酶是能够从空气中吸收N ₂并形成氨的主要酶。该酶的活性位点辅因子FeMoco在性质上是独特的。它有七个通过S桥连接的Fe和一个Mo原子，一个C原子位于辅因子的中心。另一个不寻常的特征是它具有大的均柠檬酸盐配体，已知该配体对催化很重要。在当前的计算研究中，研究了纯柠檬酸盐配体的作用。结果发现，较大的结构变化使Mo ^III处于五配位状态，在更大还原态下在能量上是有利的。这对于固氮酶机制可能很重要。

更新日期：2018-01-05

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