家蚕丝素蛋白质在不同 p H条件下经均相和不均相配位反应制备了 Cu( ) -丝素配合物 ,用可见光谱、电子自旋共振波谱 ( ESR)、 X射线衍射 ( XRD)研究了其配位结构和高次结构 .在碱性条件下 ( p H=1 0 .60 ) ,丝素肽链主链的 4个氮原子螯合 Cu( )生成具有近似平面四方 Cu( N) 4结构的配合物 ;而在酸性条件下 ( p H=4 .3 0 ,5.88) ,主要是丝素肽链的侧 (端 )基羧酸根键合 Cu( )生成 Cu( ) (—COO— ) ( H2 O) 3和 Cu( ) (— COO— ) 2 型配合物 .讨论和描述了不同条件下生成的 Cu( ) -丝素配合物的高次结构 The silk fibroin was prepared by the homogeneous and heterogeneous coordination reaction under different conditions of p H, and its structure was characterized by visible spectrum, electron spin resonance spectrum (ESR) and X-ray diffraction (XRD) (P H = 10.60). The four nitrogen atoms in the main chain of silk fibroin peptide chelated Cu () to form a Cu (N) 4 structure. Under acid conditions (p H = 4.30, 5.88), Cu () was mainly produced by the side-chain carboxylation of Cu () ) (H 2 O) 3 and Cu () (COO 2) 2 complexes are discussed and described. The higher order structure of Cu ()