摘要
采用共振拉曼光谱技术研究了细胞色素 c一次突变体 ( WT)及其二次突变体 Y67F和 N5 2 I在低频区的光谱特征 .结果表明 ,以苯丙氨酸替代 WT中酪氨酸残基 Tyr 67并没有明显影响血红素丙氨酸侧基周围多肽氨基酸残基的构象 ,而异亮氨酸对天冬酰胺残基 Asn5 2的取代则较大程度地改变了蛋白质内部水分子与周围氨基酸残基间的氢键作用和多肽空腔的疏水性 ,进而使氨基酸残基和血红素的构象相应发生调变 .
The spectroscopic characteristics of cytochrome c(WT) and its mutants(Y67F and N52I) in the low frequency region were studied by Resonance Raman technique. The results show that the replacement of phenylalanine for Tyr 67 in WT had a very slight effect on the hydrogen bonding and conformation of the amino acid residues around propionic acid side chains of heme group. However, large effects on the hydrogen bonding of internal water with its surrounding amino acid residues and hydrophobility of the heme cavity were observed as Asn 52 was substituted with isoleucine, which resulted in conformational regulations of heme group and surrounding amino acid residues.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
2002年第1期42-45,共4页
Chemical Journal of Chinese Universities
基金
国家自然科学基金 (批准号 :2 0 0 730 2 8)
苏州大学启动基金资助
