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An intramolecular disulfide bond designed in myoglobin fine-tunes both protein structure and peroxidase activity

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成果类型:
期刊论文
作者:
Wu, Lei-Bin;Yuan, Hong;Zhou, Hu;Gao, Shu-Qin;Nie, Chang-Ming;...
通讯作者:
Lin, Ying-Wu
作者机构:
[Nie, Chang-Ming; Wu, Lei-Bin; Lin, Ying-Wu] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
[Yuan, Hong; Tan, Xiangshi] Fudan Univ, Inst Biomed Sci, Shanghai Key Lab Chem Biol Prot Res, Dept Chem, Shanghai 200433, Peoples R China.
[Zhou, Hu] Chinese Acad Sci, Shanghai Inst Mat Med, CAS Key Lab Receptor Res, Dept Analyt Chem, Shanghai 201203, 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.
Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.
语种:
英文
关键词:
*Coordination state;*Disulfide bond;*Heme proteins;*Peroxidase activity;*Protein design
期刊:
Archives of Biochemistry and Biophysics
ISSN:
0003-9861
年:
2016
卷:
600
页码:
47-55
基金类别:
It is a pleasure to acknowledge Prof. S. G. Sligar and Prof. Y. Lu of University of Illinois at Urbana-Champaign, for the kind gift of sperm whale Mb gene. EPR spectra were collected at the high magnetic field laboratory of Chinese Academy of Science. NAMD and VMD were developed by the Theoretical Biophysics Group in the Beckman Institute for Advanced Science and Technology at the University of Illinois at Urbana-Champaign, USA. This work was supported by the National Science Foundation of China (No. 31370812 to Y.-W. Lin, 21472027 to X. Tan, 21375138 to H. Zhou and 11275090 to C.-M. Nie), Hunan Provincial Natural Science Foundation for Distinguished Young Scholars ( 2015JJ1012 to Y.-W. Lin) and Zhengxiang scholar program of the University of South China (Y.-W. Lin) ( 2014-003 ).
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:
Disulfide bond plays crucial roles in stabilization of protein structure and in fine-tuning protein functions. To explore an approach for rational heme protein design, we herein rationally introduced a pair of cysteines (F46C/M55C) into the scaffold of myoglobin (Mb), mimicking those in native neuroglobin. Molecular modeling suggested that it is possible for Cys46 and Cys55 to form an intramolecular disulfide bond, which was confirmed experimentally by ESI-MS analysis, DTNB reaction and CD spectrum. Moreover, it was shown that the spontaneously...

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