National Changhua University of Education Institutional Repository : Item 987654321/15148
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 6498/11670
造访人次 : 27767635      在线人数 : 181
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/987654321/15148

题名: Human Sco1 and Sco2 Function as Copper-binding Proteins
作者: Horng, Yih-Chern;Leary, Scot C.;Cobine, Paul A.;Young, Fiona B. J.;George, Graham N.;Shoubridge, Eric A.;Winge, Dennis R.
贡献者: 化學系
日期: 2005
上传时间: 2013-01-07T02:15:50Z
出版者: American Society for Biochemistry and Molecular Biology
摘要: The function of human Sco1 and Sco2 is shown to be dependent on copper ion binding. Expression of soluble domains of human Sco1 and Sco2 either in bacteria or the yeast cytoplasm resulted in the recovery of copper-containing proteins. The metallation of human Sco1, but not Sco2, when expressed in the yeast cytoplasm is dependent on the co-expression of human Cox17. Two conserved cysteines and a histidyl residue, known to be important for both copper binding and in vivo function in yeast Sco1, are also critical for in vivo function of human Sco1 and Sco2. Human and yeast Sco proteins can bind either a single Cu(I) or Cu(II) ion. The Cu(II) site yields S-Cu(II) charge transfer transitions that are not bleached by weak reductants or chelators. The Cu(I) site exhibits trigonal geometry, whereas the Cu(II) site resembles a type II Cu(II) site with a higher coordination number. To identify additional potential ligands for the Cu(II) site, a series of mutant proteins with substitutions in conserved residues in the vicinity of the Cu(I) site were examined. Mutation of several conserved carboxylates did not alter either in vivo function or the presence of the Cu(II) chromophore. In contrast, replacement of Asp238 in human or yeast Sco1 abrogated the Cu(II) visible transitions and in yeast Sco1 attenuated Cu(II), but not Cu(I), binding. Both the mutant yeast and human proteins were nonfunctional, suggesting the importance of this aspartate for normal function. Taken together, these data suggest that both Cu(I) and Cu(II) binding are critical for normal Sco function.
關聯: J. Biol. Chem., 280: 34113-34122
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.html0KbHTML524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