丝胶蛋白质与铜(Ⅱ)的配位反应  

COORDINATION REACTION OF SILK SERICIN PROTEIN WITH COPPER(Ⅱ)

作　　者：刘冠峰[1] 陈文兴[1] 傅雅琴[1] 沈之荃[2] 

机构地区：[1]浙江工程学院材料与纺织学院,杭州310033 [2]浙江大学高分子科学与工程系,杭州310027

出　　处：《高分子学报》2001年第1期58-61,共4页Acta Polymerica Sinica

基　　金：浙江省自然科学基金人才奖金资助项目(基金号RC00047)

摘　　要：本文运用pH滴定、光谱法、电子自旋波谱、X射线衍射研究丝胶蛋白质与铜 (Ⅱ )的配位反应及其络合物的高次结构 .当溶液的 pH >9 1时 ,丝胶蛋白质与Cu(Ⅱ )生成了稳定的络合物 ,此络合物具有拉伸八面体Cu(N) 4(OH-) 2 型配位结构 ,高次结构为无规卷曲非晶结构 .In order to develop and apply the silk sericin protein in functional polymeric materials, the co\| ordination reaction of sericin with copper(Ⅱ) ion in aqueous solution is studied by measurements of pH titration and optical spectra, and the coordination structure of the formed complex at high pH as well as its higher order structure are investigated by electron spin resonance(ESR) spectra and X ray diffraction. When the pH value is over 9 1 or so, each Cu 2+ consumes about four OH - ions, and the optical absorption band lies at 540nm, which indicate that the type of Cu 2+ protein biuret complex is formed. And the ESR spectrum shows that the unpaired electron of copper(Ⅱ) in the complex localizes in the ground state of d x2-y2 orbit. So it is put forward such coordination structure as Cu(N) 4(OH -) 2, whose special structure is of stretchy octahedron. The X ray diffraction pattern shows that the copper(Ⅱ) silk sericin complex has an amorphous structure of random coil.

关 键 词：丝胶 Cu(Ⅱ)-蛋白质络合物 配位结构 高次结构 

分 类 号：O629[理学—有机化学]