Cofactor-specific covalent anchoring of cytochrome b562 on a single-walled carbon nanotube by click chemistry

被引：8

作者：

Onoda, Akira ^{[1
]}

Inoue, Nozomu ^{[1
]}

Campidelli, Stephane ^{[2
]}

Hayashi, Takashi ^{[1
]}

机构：

[1] Osaka Univ, Grad Sch Engn, Dept Appl Chem, Suita, Osaka 5650871, Japan

[2] Univ Paris Saclay, CEA Saclay, CNRS, LICSEN,NIMBE,CEA, F-91191 Gif Sur Yvette, France

来源：

RSC ADVANCES | 2016年 / 6卷 / 70期

基金：

日本学术振兴会;

关键词：

DIRECT ELECTRON-TRANSFER; GLUCOSE-DEHYDROGENASE; REDOX ENZYMES; HEME-PROTEINS; RECONSTITUTION; PEROXIDASE; MYOGLOBIN; BIOELECTROCATALYSIS; IMMOBILIZATION; MONOLAYERS;

D O I：

10.1039/c6ra14195a

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Redox-active cytochrome b(562) with a tethered azide group on the heme propionate side chain is covalently linked to an acetylene moiety introduced on the sidewall of a single-walled carbon nanotube (SWNT) by copper-catalyzed click chemistry forming a triazole ring with the heme active site directly linked to the SWNT. The cytochrome b(562)-SWNT hybrid is characterized by electrochemistry and atomic force microscopy.

引用

页码：65936 / 65940

页数：5

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