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
Langmuir ◽  
1995 ◽  
Vol 11 (12) ◽  
pp. 4818-4822 ◽  
Author(s):  
Ling Sang Wong ◽  
Vincent L. Vilker ◽  
William T. Yap ◽  
Vytas Reipa

2018 ◽  
Vol 10 (44) ◽  
pp. 5297-5304 ◽  
Author(s):  
Yanyan Niu ◽  
Juan Liu ◽  
Wei Chen ◽  
Chunxiao Yin ◽  
Wenju Weng ◽  
...  

Gold nanotriangles (AuNTs) were used as a modifier on the surface of a carbon ionic liquid electrode (CILE), which was applied to realize direct electrochemistry and electrocatalysis of horseradish peroxidase (HRP).


2005 ◽  
Vol 385 (3) ◽  
pp. 745-754 ◽  
Author(s):  
Sergey SHLEEV ◽  
Andreas CHRISTENSON ◽  
Vladimir SEREZHENKOV ◽  
Dosymzhan BURBAEV ◽  
Alexander YAROPOLOV ◽  
...  

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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