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Peroxidase-like activity of L29H myoglobin with two cooperative distal histidines on electrode using O2 as an oxidant

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成果类型:
期刊论文
作者:
Dong, Shan-Shan;Du, Ke-Jie;You, Yong;Liu, Fang;Wen, Ge-Bo;...
通讯作者:
Lin, Ying-Wu
作者机构:
[Dong, Shan-Shan; Lin, Ying-Wu; Du, Ke-Jie] Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China.
[Wen, Ge-Bo; You, Yong; Liu, Fang] Univ South China, Coll Med, Hengyang 421001, Peoples R China.
[Wen, Ge-Bo; You, Yong; Lin, Ying-Wu; Liu, Fang] 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:
Heme proteins;Myoglobin;Distal histidine;DDAB;Peroxidase
期刊:
Journal of Electroanalytical Chemistry
ISSN:
1572-6657
年:
2013
卷:
708
页码:
1-6
基金类别:
National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31370812, 21101091]; Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education MinistryScientific Research Foundation for the Returned Overseas Chinese Scholars
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:
We recently showed that by introduction of a second distal histidine (Leu29 to His29 mutation) in the heme pocket of sperm whale myoglobin (Mb), L29H Mb mutant exhibits an enhanced peroxidase activity compared to wild type (WT) Mb using H2O2 as an oxidant. In this study, we further showed that when L29H Mb was immobilized in didecyldimethylammonium bromide (DDAB) on glassy carbon electrode (GCE), it can efficiently reduce O2 in aerobic buffer solution to H2O2, followed by electrode-driven oxidation of guaiacol, a common peroxidase substrate, which is more effective (∼3.6-fold at pH = 7.0) ...

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