首页> 外文期刊>The Journal of Experimental Biology >Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase
【24h】

Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase

机译:大肠杆菌ATP合酶的结构和功能的交联和电子显微镜研究

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

ATP synthase, also called F1Fo-ATPase, catalyzes the synthesis of ATP during oxidative phosphorylation. The enzyme is reversible and is able to use ATP to drive a proton gradient for transport purposes. Our work has focused on the enzyme from Escherichia coli (ECF1Fo), We have used a combination of methods to study this enzyme, including electron microscopy and chemical cross-linking. The utility of these two approaches in particular, and the important insights they give into the structure and mechanism of the ATP synthase, are reviewed. [References: 43]
机译:ATP合酶,也称为F1Fo-ATPase,在氧化磷酸化过程中催化ATP的合成。该酶是可逆的,并且能够使用ATP驱动质子梯度以进行运输。我们的工作集中在大肠杆菌中的酶(ECF1Fo),我们已经使用多种方法来研究这种酶,包括电子显微镜和化学交联。审查了这两种方法的实用性,以及它们对ATP合酶的结构和机制的重要见解。 [参考:43]

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