STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS

O. Pokidova, N. Emel'yanova, A. Kulikov, A. Kotelnikov, N. Sanina
{"title":"STUDY OF THE TRANSFORMATION OF NITROSYL IRON COMPLEX WITH N-ETHYLTHIOUREA LIGANDS IN MODEL BIOLOGICAL SYSTEMS","authors":"O. Pokidova, N. Emel'yanova, A. Kulikov, A. Kotelnikov, N. Sanina","doi":"10.47501/978-5-6044060-1-4.52","DOIUrl":null,"url":null,"abstract":"The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.","PeriodicalId":302576,"journal":{"name":"Institute of information technology","volume":"39 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"1900-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Institute of information technology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.47501/978-5-6044060-1-4.52","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

The process of transformation of a mononuclear cationic complex with N-ethylthiourea ligands in Tris-HCl buffer, as well as in a reaction mixture with reduced glutathione and bovine serum albumin, has been studied. It was found that in the presence of glutathione, the complex dimer-izes, while its initial ligands are replaced by glutathione. In the presence of albumin, the decay product of the complex is coordinated with amino acid residues (Cys34 and His39) to form a protein-bound complex.
亚硝基铁配合物与n -乙基硫脲配体在模式生物系统中的转化研究
研究了n -乙基硫脲配体单核阳离子配合物在Tris-HCl缓冲液中以及在还原型谷胱甘肽和牛血清白蛋白的反应混合物中转化的过程。发现在谷胱甘肽存在下,复合物二聚体化,而其初始配体被谷胱甘肽取代。在白蛋白存在的情况下,复合物的衰变产物与氨基酸残基(Cys34和His39)配合形成蛋白质结合复合物。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信