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我们曾研究了Cu(Ⅱ),Ni(Ⅱ),Zn(Ⅱ),Cd(Ⅱ),Hg(Ⅱ)与HSA(Human serum albumin,人血清白蛋白)和BSA(Bovin serum alburmin,牛血清白蛋白)的相互作用,鉴于锰酶和锰蛋白在生物无机化学上的重要性,且迄今未见有关Mn(Ⅱ)与HSA和BSA相互作用的研究报道,本文在紫外区观察LMCT谱带,研究了1:1 Mn(Ⅱ)-HSA和Mn(Ⅱ)-BSA在生理pH下金属中心的结构.结果表明:浓度较低时,金属中心具有五配位的四方锥构型,浓度较高时则转变为四配位的四方平面构型;结合位置最可能位于HSA和BSA的N-端三肽段上,涉及四个含氮基团,第五个配位原子是Asp~1上的羧基氧.本文还计算并讨论了Mn(Ⅱ)及有关配位原子的光学电负性.
We have studied the effects of Cu (Ⅱ), Ni (Ⅱ), Zn (Ⅱ), Cd (Ⅱ), Hg (Ⅱ) and HSA (Human serum albumin) and BSA (Bovin serum alburmin) Protein) interactions. In view of the importance of manganese and manganese proteins in bio-inorganic chemistry and so far no studies on the interaction between Mn (Ⅱ) and HSA and BSA have been reported, we observed the LMCT bands in the ultraviolet The structure of 1: 1 Mn (Ⅱ) -HSA and Mn (Ⅱ) -BSA at the pH of the metal center was studied. The results show that the metal center has a quintic tetragonal conformation at low concentration, To four-coordinate tetragonal planar configuration; the binding sites are most likely located on the N-terminal tripeptide of HSA and BSA, involving four nitrogen-containing groups, and the fifth coordinating atom is a carboxyl group on Asp ~ 1 Oxygen.In this paper, we also calculate and discuss the optical electronegativity of Mn (Ⅱ) and related coordination atoms.