绿色木霉纤维素酶分子内氢键特征的研究  

Hydrogen-Bond State Analysis of CellobiohydrolaseⅡ Molecule fromTrichoderma Viride

作　　者：余多慰[1] 袁生[1] 

机构地区：[1]南京师范大学生命科学学院,江苏南京210097

出　　处：《光谱学与光谱分析》2005年第4期544-547,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金 (30 1 70 0 0 5);江苏省高校自然科学基金 (0 3KJB1 80 0 64)资助项目

摘　　要：运用能够揭示蛋白质分子基团振动特征的激光拉曼光谱分析技术,对绿色木霉纤维素酶中的CBHⅡ在固态以及两种pH值的液态中酶分子内的氢键状态进行了分析。结果表明相对于纤维素酶固体干粉,液态中酶分子酰胺Ⅰ羰基氧原子作为氢键质子受体的能力为上升;酰胺Ⅱ与酰胺Ⅰ的β结构特征峰变化倾向相似。在3种样品中,酶蛋白中Trp均为强氢键供体,从成键能力方面证实了以往同类酶空间分析的结果。固体与pH 6 0水溶液酶蛋白中酪氨酸酚羟基成键能力也是强的。根据游离巯基分析可以判断绿色木霉CBHⅡ的成熟肽CBD与瑞氏木霉CBHⅡ的CBD有相似的二硫键构成。Hydrogen-bond states on cellobiohydrolase Ⅱ (CBHⅡ) of trichoderma viride were analysed by laser Raman spectroscopic method used to reveal molecular normal modes of vibration character. The results indicated that hydrogen-bond ability of carbonyl oxygen-atom of amideⅠ was raised in two types of aqueous solution samples(6.0 and 8.0 of pH value) compared to the solid sample. The variation trend of β structure modes was similar between amideⅡ and amideⅠ. As far as the ability of hydrogen-bond forming is concerned, tryptophan (Trp) and tyrosine (Typ) residues are strong hydrogen proton donor in pH 6.0 and solid sample, thus proving the results of previously spatial structure analysis. By analysis of free S-H character, the -S-S- construction in trichoderma viride mature paptide has been proved to be the same as that of trichoderma reesei.

关 键 词：纤维素酶 绿色木霉 分子内氢键 光谱分析技术 成键能力 激光拉曼 振动特征 分子基团 质子受体 空间分析 瑞氏木霉 酶蛋白 CBD 蛋白质 pH值 氧原子 酰胺 酶分子 特征峰 β结构 Trp 酚羟基 酪氨酸 水溶液 二硫键 成熟肽 液态 

分 类 号：O623.413[理学—有机化学] TQ925.9[理学—化学]