首页> 外文期刊>FEBS letters. >Detecting transient protein-protein interactions by X-ray absorption spectroscopy: The cytochrome c(6)-photosystem I complex
【24h】

Detecting transient protein-protein interactions by X-ray absorption spectroscopy: The cytochrome c(6)-photosystem I complex

机译:通过X射线吸收光谱法检测瞬态蛋白质-蛋白质相互作用:细胞色素c(6)-光系统I复合物

获取原文
获取原文并翻译 | 示例
获取外文期刊封面目录资料

摘要

Reliable analysis of the functionality of metalloproteins demands a highly accurate description of both the redox state and geometry of the metal centre, not only in the isolated metalloprotein but also in the transient complex with its target. Here, we demonstrate that the transient interaction between soluble cytochrome c(6) and membrane-embedded photosystem I involves subtle changes in the heme iron, as inferred by X-ray absorption spectroscopy (XAS). A slight shift to lower energies of the absorption edge of Fe2+ in cytochrome c(6) is observed upon interaction with photosystem I. This work constitutes a novel application of XAS to the analysis of weak complexes in solution. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
机译:要可靠地分析金属蛋白的功能,不仅需要在分离的金属蛋白中而且还要在与靶标形成的瞬态复合物中对金属中心的氧化还原状态和几何中心进行高度准确的描述。在这里,我们证明了可溶性细胞色素c(6)和膜嵌入的光系统I之间的瞬时相互作用涉及血红素铁的细微变化,如X射线吸收光谱法(XAS)所推断的。与光系统​​I相互作用时,观察到细胞色素c(6)中Fe2 +吸收边缘的较低能量略有转移。这项工作构成了XAS在溶液中弱复合物分析方面的新应用。 (c)2006年欧洲生物化学学会联合会。由Elsevier B.V.发布。保留所有权利。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号