氧化亞氮還原酶(Nitros Oxide Reductase,N2OR)的催化作用是 在常溫常壓下將N2O還原成N2和H2O。目前已被確認在不同種類的去 氧菌(denitrifying bacteria)中並且已從生物體中解析出晶體結構,得 知他的活性中心是由CuA與CuZ所組成。而與N2O有反應活性的是在 CuZ上以一個硫作為中心周圍圍繞著四個銅一價的活性中心,然而, N2O如何與活性中心鍵結與催化的機制至今仍不清楚。 我們合成一系列利用[tris(2-pyridylmethyl)amine] (tmpa)作為配位 基的起始物,並且我們發現在Kenneth D. Karlin模擬生物活性中也有 用相同配位基。但是有許多基本的化學問題尚未解決並且與我們的起 始物有類似的特性引起我們的興趣,我們合成出來的[(tmpa)CuCl](1) 有著流變現象,在室溫中的NMR儀器分析中發現,無法得到正確分 裂的鋒,必須降到低溫才能偵測到完整的訊號分裂。因此我們合成出 [(tmpa)CuBr](2)、[(tmpa)CuI](3)、[(tmpa)Cu(PPh3)Cl](5)、 [(tmpa)Cu(MeCN)]BPh4(8)、[(tmpa)Cu(CNArCN)]Cl(9),來探討他在 室溫中正確的結構變化;並且再利用[(tmpa)CuCl](1)與氣體CO與N2O 反應並且探討其是否有反應活性。
Nitros Oxide Reductase, N2OR, catalyze the reduction of N2O into N2 and water under ambient temperature and pressure. N2OR have already been confirmed by crystallography at present, it is learnt that the active centre consists of CuA and CuZ. The active site with N2O is to regard a piece of sulfide around four pieces of copper(I) around the centre on CuZ, however, not yet clear so far how N2O forms the mechanism with the catalysis with the active centre key. A series of [tris(2-pyridylmethyl)amine] (tmpa) as the ligand of the coordinating, and we find the base of coordinating usefully and the same study in the biological modeling. On the other side, there are a lot of basic chemical problems have not been solved yet and have similar characteristics to interest us with our ligand. That come out [(tmpa)CuCl](1) have fluxional behavior, found NMR instrument on room temperature in not analyzing, it is unable to get the correct sharp peak that split. We format [(tmpa)CuBr](2), [(tmpa)CuI](3), [(tmpa)Cu(PPh3)Cl](5), [(tmpa)Cu(MeCN)]BPh4(8), [(tmpa)Cu(CNArCN)]Cl(9), it come to explain into how the being at room temperature correct structure change and the mechanism, and [(tmpa)CuCl](1) react with CO and N2O to find out that whether our chemical compound has activation.