期刊
FARADAY DISCUSSIONS
卷 145, 期 -, 页码 301-313出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/b907121k
关键词
-
资金
- Deutsche Forschungsgemeinschaft (DFG) [Zi 436/13-1, SFB 739]
The thermodynamic stability of radicals involved in enzymatic catalysis has been quantified using a series of theoretical methods. It is found that three of the most often encountered radicals located on the enzyme protein chain (tyrosyl, cysteinyl and glycyl radicals) are of similar stability. This is despite the fact that O-H, S-H and C-H bonds have intrinsically very different homolytic bond dissociation energies. The cofactor-derived 5'-adenosyl radical, in contrast, is significantly less stable than these protein-bound radicals.
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