Formation of Cys-heme cross-link in K42C myoglobin under reductive conditions with molecular oxygen

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成果类型：

期刊论文

作者：

Cheng, Hui-Min;Yuan, Hong;Wang, Xiao-Juan;Xu, Jia-Kun;Gao, Shu-Qin;...

通讯作者：

Lin, Ying-Wu

作者机构：

[Lin, Ying-Wu; Wang, Xiao-Juan; Cheng, Hui-Min] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.

[Yuan, Hong; Tan, Xiangshi] Fudan Univ, Shanghai Key Lab Chem Biol Prot Res, Dept Chem, Shanghai 200433, Peoples R China.

[Yuan, Hong; Tan, Xiangshi] Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China.

[Xu, Jia-Kun] Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China.

[Gao, Shu-Qin; Wen, Ge-Bo; Lin, Ying-Wu] Univ South China, Lab Prot Struct & Funct, 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：

*Cross-link;*Heme proteins;*Mechanism;*Protein design;*X-ray crystallography

期刊：

Journal of Inorganic Biochemistry

ISSN：

0162-0134

年：

2018

卷：

182

页码：

141-149

DOI：

10.1016/j.jinorgbio.2018.02.011

基金类别：

National Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31370812, 21701081]; Hunan Provincial Natural Science FoundationNatural Science Foundation of Hunan Province [2015JJ1012]; Scientific Research Fund of Hunan Provincial Education DepartmentHunan Provincial Education Department [15A158, 14C1004]; USC

机构署名：

本校为第一且通讯机构

院系归属：

化学化工学院

摘要：

The structure and function of heme proteins are regulated by diverse post-translational modifications including heme-protein cross-links, with the underlying mechanisms not well understood. In this study, we introduced a Cys (K42C) close to the heme 4-vinyl group in sperm whale myoglobin (Mb) and solved its X-ray crystal structure. Interestingly, we found that K42C Mb can partially form a Cys-heme cross-link (termed K42C Mb-X) under dithiothreitol-induced reductive conditions in presence of O 2 , as suggested by guanidine hydrochloride-induced ...

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Formation of Cys-heme cross-link in K42C myoglobin under reductive conditions with molecular oxygen

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