The importance of Asn52 in the structure-function relationship of human cytochrome c

被引：10
作者：
Lou, Dan [1 ]
Liu, Xi-Chun [1 ]
Wang, Xiao-Juan [1 ]
Gao, Shu-Qin [2 ]
Wen, Ge-Bo [2 ]
Lin, Ying-Wu [1 ,2 ]
机构：
[1] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China
[2] Univ South China, Lab Prot Struct & Funct, Med Sch, Hengyang 421001, Peoples R China
来源：
RSC ADVANCES | 2020年 / 10卷 / 73期
基金：
中国国家自然科学基金;
关键词：
PEROXIDASE-ACTIVITY; TYROSINES; 46; STATE; NITRATION; DYNAMICS; MUTATION; VARIANT; ACTIVATION; STABILITY; APOPTOSIS;
D O I：
10.1039/d0ra09961a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The function of the highly conserved residue Asn52 in human cytochrome c (H-Cyt c) is not fully understood. Herein, we show that the naturally occurring variant N52S H-Cyt c has a perturbed secondary structure, with a small fraction of high-spin species. Remarkably, it exhibits an enhanced peroxidase activity by 3-8-fold at neutral pH, as well as self-oxidation in reaction with H2O2. This study suggests that the H-bond network mediated by Asn52 is essential to suppress the apoptotic activity of H-Cyt c under physiological conditions.
引用
收藏
页码：44768 / 44772
页数：5
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