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学科主题: 分析化学
题名: Study on the gas phase stability of heme-binding pocket in cytochrome Tb^5 and its mutants by electrosprary mass spectrometry
其他题名: 电喷雾质谱法研究细胞色素Tb5和野生型稳定性
作者: Yu CT(余翀天) ; Guo YL(郭寅龙) ; Lv L(吕龙) ; Wang YH(王韵华) ; Yao P(姚萍) ; Huang ZX(黄仲贤)
通讯作者: 郭寅龙
刊名: Chin. J. Chem.
发表日期: 2002-01-01
卷: 20, 期:12, 页:1540-1545
收录类别: SCI
部门归属: 中国科学院上海有机化学研究所分析化学实验室; 复旦大学
英文摘要: To elucidate the effect of various amino acid residues on the heme-binding pocket in cytochrome Tb^5, several residues were chosen for replacement by means of site-directed mutagenesis. Comparison of the mass spectrum between the F35Y mutant and the wild type shows that the relative abundance of holoprotein ion of F35Y is lower than that of the wild type in gas phase. It is concluded that mutation from Phe35 residue to tyrosine decreses the hydrophobic character of cytochrome Tb5 heme pocket, which decreases the stability of heme-binding pocket. ESI_MS spectra of the mutants V61E, V61K, V61H and V61Y show various contribution of amino acid to the stability of heme-binding pocket. The small and non-polar residue Val61 was replaced with large or polar residues, resulting in enhancing the trend of heme leaving from the pocket. In addition, comparion of the mass relative abundance of holo-proteins among all the Val61-mutants, shows that their stability in gas phase appropriately submit the following order: wild type >V61H>>V61E>>V61K≈>V61Y. The extra great stability of quadruple sites mutant E44/48/56A/D60A shofws that reduction of electrostatic or hydrogen bond interactions among the residues locating in the outside region of the heme edge remarkably affect the stability of heme. The results of ananlyzing the oxidation states of heme iron in Tb^5 and its mutants by insource-CAD experiment suggest that the charge states of heme iron maintain inflexible in mutaion process.
语种: 英语
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/19812
Appears in Collections:分析化学研究室_期刊论文

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Recommended Citation:
Yu CT,Guo YL,Lv L,et al. Study on the gas phase stability of heme-binding pocket in cytochrome Tb^5 and its mutants by electrosprary mass spectrometry[J]. Chin. J. Chem.,2002,20(12):1540-1545.
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