采用密度泛函活性理论研究了以锌指蛋白为基础建立的3种锌指模型,MS4-xNx(M为二价金属离子Mg,Ca,Sc,Ti,V,Cr,Mn,Fe,Co,Ni,Cu,Zn;S和N分别代表组氨酸和半胱氨酸残基;x=0,1,2),并探讨了其金属结合特异性.结果表明,当锌离子参与键合时,体系既表现出最大稳定性,同时又显示出最大反应活性.这种同时把稳定性和反应活性有机地结合于一体的特质清楚地说明了锌指蛋白质分子对金属锌离子键合的专一性. Three kinds of zinc finger models based on zinc finger protein were studied using density functional theory. MS4-xNx (M is a divalent metal ion such as Mg, Ca, Sc, Ti, V, Cr, Mn, Fe, Co, Ni, Cu, Zn; S and N represent histidine and cysteine ​​residues, respectively; x = 0, 1 and 2), and their metal-binding specificity was also discussed.The results showed that when zinc ions were involved in the bonding , The system shows both maximum stability and maximum reactivity at the same time.The combination of stability and reactivity at the same time clearly shows that the zinc finger protein molecules are specific to metal zinc ion bonding Sex.