National Changhua University of Education Institutional Repository : Item 987654321/15468
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 6507/11669
造访人次 : 29726513      在线人数 : 575
RC Version 3.2 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 进阶搜寻

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://ir.ncue.edu.tw/ir/handle/987654321/15468

题名: Ultrafast Solvation Dynamics at Binding and Active Sites of Photolyases
作者: Chang, Chih-Wei;Guo, Lijun;Kao, Ya-Ting;Li, Jiang;Tan, Chuang;Li, Tanping;Saxena, Chaitanya;Liu, Zheyun;Wang, Lijuan;Sancar, Aziz;Zhong, Dongping
贡献者: 化學系
日期: 2010-02
上传时间: 2013-02-05T02:21:30Z
出版者: the National Academy of Sciences
摘要: Dynamic solvation at binding and active sites is critical to protein recognition and enzyme catalysis. We report here the complete characterization of ultrafast solvation dynamics at the recognition site of photoantenna molecule and at the active site of cofactor/substrate in enzyme photolyase by examining femtosecond-resolved fluorescence dynamics and the entire emission spectra. With direct use of intrinsic antenna and cofactor chromophores, we observed the local environment relaxation on the time scales from a few picoseconds to nearly a nanosecond. Unlike conventional solvation where the Stokes shift is apparent, we observed obvious spectral shape changes with the minor, small, and large spectral shifts in three function sites. These emission profile changes directly reflect the modulation of chromophore’s excited states by locally constrained protein and trapped-water collective motions. Such heterogeneous dynamics continuously tune local configurations to optimize photolyase’s function through resonance energy transfer from the antenna to the cofactor for energy efficiency and then electron transfer between the cofactor and the substrate for repair of damaged DNA. Such unusual solvation and synergetic dynamics should be general in function sites of proteins.
關聯: Proceedings of The National Academy of Sciences, 107(7): 2914-2919
显示于类别:[化學系] 期刊論文

文件中的档案:

档案 大小格式浏览次数
index.html0KbHTML723检视/开启


在NCUEIR中所有的数据项都受到原著作权保护.

 


DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回馈