scholarly journals Redox potentials of the blue copper sites of bilirubin oxidases

2006 ◽  
Vol 1757 (12) ◽  
pp. 1634-1641 ◽  
Author(s):  
Andreas Christenson ◽  
Sergey Shleev ◽  
Nicolas Mano ◽  
Adam Heller ◽  
Lo Gorton
1996 ◽  
Vol 243 (1-2) ◽  
pp. 67-78 ◽  
Author(s):  
Edward I. Solomon ◽  
Kevin W. Penfield ◽  
Andrew A. Gewirth ◽  
Michael D. Lowery ◽  
Susan E. Shadle ◽  
...  

2003 ◽  
Vol 8 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Claudio O. Fernández ◽  
Tomotake Niizeki ◽  
Takamitsu Kohzuma ◽  
Alejandro J. Vila

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.


1992 ◽  
Vol 47 (3-4) ◽  
pp. 26
Author(s):  
Joann Sanders-Loehr
Keyword(s):  

Sign in / Sign up

Export Citation Format

Share Document