Characterization of Mercaptoethylamine-Modified Gold Electrode Surface and Analyses of Direct Electron Transfer to Putidaredoxin

Langmuir ◽  
1995 ◽  
Vol 11 (12) ◽  
pp. 4818-4822 ◽  
Author(s):  
Ling Sang Wong ◽  
Vincent L. Vilker ◽  
William T. Yap ◽  
Vytas Reipa
Keyword(s):  
Electron Transfer ◽  
Electrode Surface ◽  
Gold Electrode ◽  
Direct Electron Transfer

Direct electron transfer of horseradish peroxidase on Nafion-cysteine modified gold electrode

2007 ◽  
Vol 52 (21) ◽  
pp. 6261-6267 ◽  
Author(s):  
Jun Hong ◽  
Ali Akbar Moosavi-Movahedi ◽  
Hedayatollah Ghourchian ◽  
Ahmad Molaei Rad ◽  
Saeed Rezaei-Zarchi
Keyword(s):  
Electron Transfer ◽  
Horseradish Peroxidase ◽  
Gold Electrode ◽  
Direct Electron Transfer

scholarly journals Recent Advances in the Direct Electron Transfer-Enabled Enzymatic Fuel Cells

2021 ◽  
Vol 8 ◽  
Author(s):  
Sooyoun Yu ◽  
Nosang V. Myung
Keyword(s):  
Electron Transfer ◽  
Fuel Cell ◽  
Active Site ◽  
Electrode Surface ◽  
Oxidation Reaction ◽  
Direct Electron Transfer ◽  
Implantable Devices ◽  
Protein Matrix ◽  
Enzyme Active Site ◽  
Enzymatic Fuel Cell

Direct electron transfer (DET), which requires no mediator to shuttle electrons from enzyme active site to the electrode surface, minimizes complexity caused by the mediator and can further enable miniaturization for biocompatible and implantable devices. However, because the redox cofactors are typically deeply embedded in the protein matrix of the enzymes, electrons generated from oxidation reaction cannot easily transfer to the electrode surface. In this review, methods to improve the DET rate for enhancement of enzymatic fuel cell performances are summarized, with a focus on the more recent works (past 10 years). Finally, progress on the application of DET-enabled EFC to some biomedical and implantable devices are reported.

scholarly journals Direct Electron Transfer-Type Bioelectrocatalysis of Redox Enzymes at Nanostructured Electrodes

Catalysts ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 236 ◽  
Author(s):  
Taiki Adachi ◽  
Yuki Kitazumi ◽  
Osamu Shirai ◽  
Kenji Kano
Keyword(s):  
Electron Transfer ◽  
Protein Engineering ◽  
Electrode Surface ◽  
Direct Electron Transfer ◽  
Redox Enzymes ◽  
Type Reaction ◽  
The Past ◽  
Electrode Reactions ◽  
Basic Concepts ◽  
Catalytic Functions

Direct electron transfer (DET)-type bioelectrocatalysis, which couples the electrode reactions and catalytic functions of redox enzymes without any redox mediator, is one of the most intriguing subjects that has been studied over the past few decades in the field of bioelectrochemistry. In order to realize the DET-type bioelectrocatalysis and improve the performance, nanostructures of the electrode surface have to be carefully tuned for each enzyme. In addition, enzymes can also be tuned by the protein engineering approach for the DET-type reaction. This review summarizes the recent progresses in this field of the research while considering the importance of nanostructure of electrodes as well as redox enzymes. This review also describes the basic concepts and theoretical aspects of DET-type bioelectrocatalysis, the significance of nanostructures as scaffolds for DET-type reactions, protein engineering approaches for DET-type reactions, and concepts and facts of bidirectional DET-type reactions from a cross-disciplinary viewpoint.

scholarly journals Electrochemical redox transformations of T1 and T2 copper sites in native Trametes hirsuta laccase at gold electrode

2005 ◽  
Vol 385 (3) ◽  
pp. 745-754 ◽  
Author(s):  
Sergey SHLEEV ◽  
Andreas CHRISTENSON ◽  
Vladimir SEREZHENKOV ◽  
Dosymzhan BURBAEV ◽  
Alexander YAROPOLOV ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Gold Electrode ◽  
Direct Electron Transfer ◽  
High Potential ◽  
Redox Potentials ◽  
Hydrogen Electrode ◽  
Trametes Hirsuta ◽  
Redox Transformations ◽  
Copper Site ◽  
Copper Sites

Mediatorless, electrochemically driven, redox transformations of T1 (type 1) and T2 copper sites in Trametes hirsuta laccase were studied by cyclic voltammetry and spectroelectrochemical redox titrations using bare gold electrode. DET (direct electron transfer) between the electrode and the enzyme was observed under anaerobic conditions. From analysis of experimental data it is concluded that the T2 copper site is in DET contact with gold. It was found that electron transfer between the gold surface and the T1 copper site progresses through the T2 copper site. From EPR measurements and electrochemical data it is proposed that the redox potential of the T2 site for high-potential ‘blue’ laccase is equal to about 400 mV versus NHE (normal hydrogen electrode) at pH 6.5. The hypothesis that the redox potentials of the T2 copper sites in low- and high-potential laccases/oxidases from totally different sources might be very similar, i.e. approx. 400 mV, is discussed.

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