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Peroxidase activity enhancement of myoglobin by two cooperative distal histidines and a channel to the heme pocket

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成果类型:
期刊论文、会议论文
作者:
Wu, Lei-Bin;Du, Ke-Jie;Nie, Chang-Ming;Gao, Shu-Qin;Wen, Ge-Bo;...
通讯作者:
Lin, Ying-Wu
作者机构:
[Nie, Chang-Ming; Wu, Lei-Bin; Lin, Ying-Wu; Du, Ke-Jie] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
[Gao, Shu-Qin; Wen, Ge-Bo; Lin, Ying-Wu] Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.
[Tan, Xiangshi] Fudan Univ, Dept Chem, Shanghai Key Lab Chem Biol Prot Res, Shanghai 200433, Peoples R China.
[Tan, Xiangshi] Fudan Univ, Inst Biomed Sci, Shanghai 200433, 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:
Heme proteins;Peroxidase;Protein design;Cooperativity;Channel
期刊:
Journal of Molecular Catalysis B: Enzymatic
ISSN:
1381-1177
年:
2016
卷:
134
页码:
367-371
会议名称:
8th Meeting on OxiZymes
会议时间:
JUL 03-06, 2016
会议地点:
Wageningen, NETHERLANDS
会议主办单位:
[Wu, Lei-Bin;Du, Ke-Jie;Nie, Chang-Ming;Lin, Ying-Wu] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.^[Gao, Shu-Qin;Wen, Ge-Bo;Lin, Ying-Wu] Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China.^[Tan, Xiangshi] Fudan Univ, Dept Chem, Shanghai Key Lab Chem Biol Prot Res, Shanghai 200433, Peoples R China.^[Tan, Xiangshi] Fudan Univ, Inst Biomed Sci, Shanghai 200433, Peoples R China.
会议赞助商:
COST Act Syst Biocatalysis
出版地:
PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
出版者:
ELSEVIER SCIENCE BV
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:
To reveal the structure-function relationship of heme proteins, and to provide clues for creating artificial heme proteins with improved functions, we here use myoglobin (Mb) as a model protein, and report that its peroxidase activity can be enhanced by construction of two distal histidines and a channel to the heme pocket. It showed that in addition to a single distal histidine with a suitable distance to the heme iron (Phe43 to His43 mutation), a second distal histidine (Leu29 to His29 mutation) can work cooperatively to increase the turnover number, mimicking the role of well-known His-Arg ...

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