古菌型 Rieske [2Fe-2S] 中心完全去质子化、还原形式的 15N HYSCORE 表征。
15N HYSCORE characterization of the fully deprotonated, reduced form of the archaeal Rieske [2Fe-2S] center.
作者信息
Iwasaki Toshio, Kounosu Asako, Samoilova Rimma I, Dikanov Sergei A
机构信息
Department of Biochemistry and Molecular Biology, Nippon Medical School, Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan.
出版信息
J Am Chem Soc. 2006 Feb 22;128(7):2170-1. doi: 10.1021/ja0562393.
The hyperfine couplings for strongly and weakly coupled 15N nuclei around a reduced Rieske [2Fe-2S] center of uniformly 15N-labeled, hyperthermostable archaeal Rieske protein at pH 13.3 were determined by hyperfine sublevel correlation (HYSCORE) spectroscopy and compared with those at physiological pH. Significant changes in the hyperfine couplings of the terminal histidine Ndelta ligands and Nepsilon nuclei were observed between them, which can be explained by not only the redistribution of the unpaired electron spin density over the ligands but also the difference in the mixed-valence state of the fully deprotonated, reduced cluster. These quantitative data can be used in theoretical analysis for the selection of an appropriate model of the mixed-valence state of the reduced Rieske center at very alkaline pH.
通过超精细亚能级相关（HYSCORE）光谱法测定了在pH 13.3条件下，均匀15N标记的超嗜热古菌 Rieske 蛋白的还原型 Rieske [2Fe-2S] 中心周围强耦合和弱耦合15N 核的超精细耦合，并与生理pH条件下的情况进行了比较。在两者之间观察到末端组氨酸Nδ配体和Nε核的超精细耦合有显著变化，这不仅可以通过未配对电子自旋密度在配体上的重新分布来解释，还可以通过完全去质子化的还原簇的混合价态差异来解释。这些定量数据可用于理论分析，以选择在非常碱性pH条件下还原型 Rieske 中心混合价态的合适模型。
Zotero 插件