Glucose Oxidase Catalyzed Self-Assembly of Bioelectroactive Gold Nanostructures

被引:14
|
作者
Luckarift, Heather R. [1 ,2 ]
Ivnitski, Dmitri [3 ]
Rincon, Rosalba [3 ]
Atanassov, Plamen [3 ]
Johnson, Glenn R. [1 ]
机构
[1] USAF, Res Lab, Microbiol & Appl Biochem AFRL RXQL, Tyndall AFB, FL 32403 USA
[2] Universal Technol Corp, Dayton, OH 45432 USA
[3] Univ New Mexico, Dept Chem & Nucl Engn, Albuquerque, NM 87131 USA
关键词
Gold reduction; Glucose oxidase; Electron transfer; Nanocomposites; Self-assembly; DIRECT ELECTRON-TRANSFER; CARBON NANOTUBES; EXTRACELLULAR SYNTHESIS; ENZYMATIC-ACTIVITY; NANOPARTICLES; ENZYMES; NANOBIOTECHNOLOGY; BIOSYNTHESIS; ENTRAPMENT; SYSTEMS;
D O I
10.1002/elan.200980003
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Glucose oxidase catalyzes the formation of metallic gold particles in immediate proximity of the protein from gold (III) chloride in the absence of any other catalytic or reductive substrates. The protein-mediated gold reduction reaction leads to size-controllable gold particle formation and concomitant association of the enzyme in an electrically conductive metallic template. Such an enzyme immobilization strategy provides a simple and rapid method to create an intimate interface between glucose oxidase and a conductive matrix, which can be joined to an electrode surface. Model electrodes were prepared by entraining the glucose oxidase/gold particles onto carbon paper. Voltammetry of the resulting electrodes revealed stable oxidation and reduction peaks at a potential close to that of the standard value for the FAD/FADH(2) cofactor of immobilized glucose oxidase. The gold electrodes exhibit catalytic activity in the presence of glucose confirming the entrapment of active glucose oxidase within the gold architecture. The resulting composite material can be successfully integrated with electrodes of various designs for biosensor and biofuel cell applications.
引用
收藏
页码:784 / 792
页数:9
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