Cu2+与烟草多酚氧化酶相互作用研究
Study on the Interaction between Cu2+ and Polyphenol Oxidase from Nicotinna Tobaccum
作者单位
肖厚荣 中国科学技术大学化学系合肥 230026 
施春华 中国科学技术大学化学系合肥 230026 
夏炳乐 中国科学技术大学化学系合肥 230026 
盛良全 中国科学技术大学化学系合肥 230026 
张艳鸽 中国科学技术大学化学系合肥 230026 
刘清亮 中国科学技术大学化学系合肥 230026 
摘要: 本文通过酶活性测定,荧光光谱和紫外光谱研究了外加Cu2+与烟草多酚氧化酶(简称PPO)的相互作用。结果表明,微量铜的加入能增加酶的活性,[Cu2+]/[PPO]为0.20左右时酶活性最大,[Cu2+]/[PPO]为0.91时,Cu2+开始表现出对PPO活性的抑制;Cu2+对PPO内源荧光的猝灭机制属于形成络合物所引起的静态猝灭,猝灭常数Ksv为8.0375×103L·mol-1;Cu2+的加入使PPO蛋白质分子构象发生变化,α-螺旋含量增加,多肽链及Trp和Tyr残基的芳杂环进一步向分子内收缩,疏水基团之间的疏水作用增强。
关键词: 铜 多酚氧化酶 荧光光谱 紫外光谱
基金项目: 
Abstract: The interaction between Cu2+ and PPO(polyphenol oxidase) has been studied by employing enzymatic activity assay, fluorescence spectroscopy and UV/Visible spectroscopy. The results show that the activity of PPO was en-hanced by the addition of Cu2+, reaching maximum when [Cu2+]/[PPO] was about 0.20, and then, the inhibition for it was appeared due to the existence of Cu2+. The quenching mechanism of the combination of Cu2+ with PPO is a static quenching procedure, the quenching constant Ksv is 8.0375×103L·mol-1. The conformation of PPO is changed, the α-helix content is increased, the polypeptide chain and the aromatic ring in Trp and Tyr residues are contracted to the inner of molecule, the hydrophobic interaction among hydrophobic groups enhanced after Cu2+ was added to it.
Keywords: Cu2+ polyphenol oxidase fluorescence spectroscopy UV/Visible spectroscopy
 
摘要点击次数:  1370
全文下载次数:  2341
肖厚荣,施春华,夏炳乐,盛良全,张艳鸽,刘清亮.Cu2+与烟草多酚氧化酶相互作用研究[J].无机化学学报,2003,19(6):589-593.
查看全文  查看/发表评论  下载PDF阅读器
Support information: