Improved direct electron transfer-type bioelectrocatalysis of bilirubin oxidase using porous gold electrodes

2019 ◽  
Vol 843 ◽  
pp. 47-53 ◽  
Author(s):  
Yui Takahashi ◽  
Mizue Wanibuchi ◽  
Yuki Kitazumi ◽  
Osamu Shirai ◽  
Kenji Kano
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Gold Electrodes ◽  
Bilirubin Oxidase ◽  
Porous Gold

scholarly journals Direct electron transfer from graphite and functionalized gold electrodes to T1 and T2/T3 copper centers of bilirubin oxidase

2008 ◽  
Vol 1777 (10) ◽  
pp. 1364-1369 ◽  
Author(s):  
Pablo Ramírez ◽  
Nicolas Mano ◽  
Rafael Andreu ◽  
Tautgirdas Ruzgas ◽  
Adam Heller ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Gold Electrodes ◽  
Bilirubin Oxidase ◽  
T1 And T2

scholarly journals Impact of Surface Modification with Gold Nanoparticles on the Bioelectrocatalytic Parameters of Immobilized Bilirubin Oxidase

Acta Naturae ◽  
2014 ◽  
Vol 6 (1) ◽  
pp. 102-106 ◽  
Author(s):  
D. V. Pankratov ◽  
Y. S. Zeifman ◽  
А. V. Dudareva ◽  
G. K. Pankratova ◽  
M. E. Khlupova ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Electron Transfer ◽  
Transfer Rate ◽  
Direct Electron Transfer ◽  
Electron Transfer Rate ◽  
Bilirubin Oxidase ◽  
Heterogeneous Electron Transfer ◽  
Enzyme Molecules ◽  
Different Diameters ◽  
The Impact

We unveil experimental evidence that put into question the widely held notion concerning the impact of nanoparticles on the bioelectrocatalytic parameters of enzymatic electrodes. Comparative studies of the bioelectrocatalytic properties of fungal bilirubin oxidase from Myrothecium verrucaria adsorbed on gold electrodes, modified with gold nanoparticles of different diameters, clearly indicate that neither the direct electron transfer rate (standard heterogeneous electron transfer rate constants were calculated to be 319 s -1) nor the biocatalytic activity of the adsorbed enzyme (bioelectrocatalytic constants were calculated to be 3411 s -1) depends on the size of the nanoparticles, which had diameters close to or larger than those of the enzyme molecules.

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