Sulfide release and rebinding in the mechanism for nitrogenase,Journal of Computational Chemistry

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Sulfide release and rebinding in the mechanism for nitrogenase
Journal of Computational Chemistry ( IF 3.4 ) Pub Date : 2024-08-27 , DOI: 10.1002/jcc.27494
Per E M Siegbahn ₁

Affiliation

Nitrogenases are the only enzymes that activate the strong triple bond in N₂. The mechanism for the activation has been very difficult to determine in spite of decades of work. In previous modeling studies it has been suggested that the mechanism for nitrogen activation starts out by four pre-activation steps (A₀–A₄) before catalysis. That suggestion led to excellent agreement with experimental Elecrtron Paramagnetic Resonance (EPR) observations in the step where N₂ becomes protonated (E₄). An important part of the pre-activation is that a sulfide is released. In the present paper, the details of the pre-activation are modeled, including the release of the sulfide. Several possible transition states for the release have been obtained. An A₄(E₀) state is reached which is very similar to the E₄ state. For completeness, the steps going back from A₄(E₀) to A₀ after catalysis are also modeled, including the insertion of a sulfide.

中文翻译：

硫化物释放和再结合在固氮酶机制中

固氮酶是唯一激活 N₂ 中强三键的酶。尽管进行了数十年的工作，但激活的机制一直很难确定。在以前的建模研究中，有人提出氮活化的机制从催化前的四个预活化步骤（A_0-A ₄）开始。该建议导致与 N₂ 变成质子化（E₄）的步骤中的实验 Elecrtron 顺磁共振（EPR）观测结果非常一致。预活化的一个重要部分是释放硫化物。在本文中，对预活化的细节进行了建模，包括硫化物的释放。已获得该版本的几种可能的过渡状态。达到 A₄ （E₀）状态，这与 E₄ 状态非常相似。为了完整起见，还对催化后从 A₄（E₀）返回到 A₀ 的步骤进行了建模，包括硫化物的插入。

更新日期：2024-08-27

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