期刊
FEBS LETTERS
卷 579, 期 30, 页码 6875-6878出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2005.11.036
关键词
ATP binding; regulation; inhibitor; ATP synthase; F0F1
Previously, we demonstrated ATP binding to the isolated E subunit of F-1-ATPase from thermophilic Bacillus PS3 [Kato-Yamada Y., Yoshida M. (2003) J. Biol. Chem. 278, 36013]. However, whether it is a general feature of the F. subunit from other sources is yet unclear. Here, using a sensitive method to detect weak interactions between fluorescently labeled F subunit and nucleotide, it was shown that the E subunit of F-1-ATPase from Bacillus subtilis also bound ATP. The dissociation constant for ATP binding at room temperature was calculated to be 2 mM, which may be suitable for sensing cellular ATP concentration in vivo. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据