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A spectroscopic study of uranyl-cytochrome b5/cytochrome c interactions

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成果类型:
期刊论文
作者:
Sun, Mei-Hui;Liu, Shuang-Quan;Du, Ke-Jie;Nie, Chang-Ming;Lin, Ying-Wu*
通讯作者:
Lin, Ying-Wu
作者机构:
[Nie, Chang-Ming; Lin, Ying-Wu; Sun, Mei-Hui; Du, Ke-Jie] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
[Liu, Shuang-Quan] Univ South China, Affiliated Hosp 1, Dept Clin Lab, Hengyang 421001, Peoples R China.
通讯机构:
[Lin, Ying-Wu] U
Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
语种:
英文
关键词:
Uranium;Heme protein;Protein-protein interaction;Fluorescence;Peroxidase
期刊:
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
ISSN:
1386-1425
年:
2014
卷:
118
页码:
130-137
基金类别:
National Natural Science Foundation of China, NSFCNational Natural Science Foundation of China (NSFC) [21101091, 11275090]
机构署名:
本校为第一且通讯机构
院系归属:
化学化工学院
医学院
摘要:
Uranium is harmful to human health due to its radiation damage and the ability of uranyl ion (UO22+) to interact with various proteins and disturb their biological functions. Cytochrome b5 (cyt b5) is a highly negatively charged heme protein and plays a key role in mediating cytochrome c (cyt c) signaling in apoptosis by forming a dynamic cyt b 5-cyt c complex. In previous molecular modeling study in combination with UV-Vis studies, we found that UO22+ is capable of binding to cyt b 5 at surface residues, Glu37 and Glu43. In this study, we further investigated the structural consequences of cy...

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