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

Shleev, Sergey LU ; Christenson, Andreas LU ; Serezhenkov, V; Burbaev, D; Yaropolov, A; Gorton, Lo LU and Ruzgas, Tautgirdas LU (2005) In Biochemical Journal 385(Part 3). p.745-754
Abstract
Mediatorless, electrochemically driven, redox transformations of TI (type 1) and T2 copper sites in Trametes hirsuta laccase were studied by cyclic voltarnmetry and spectroclectrochernical redox titrations using bare gold electrode. DET (direct electron transfer) between I he 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 TI 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... (More)
Mediatorless, electrochemically driven, redox transformations of TI (type 1) and T2 copper sites in Trametes hirsuta laccase were studied by cyclic voltarnmetry and spectroclectrochernical redox titrations using bare gold electrode. DET (direct electron transfer) between I he 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 TI 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-potentiai laccases/oxiclases from totally different sources might be very similar, i.e. approx. 400 mV, is discussed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical Journal
volume
385
issue
Part 3
pages
745 - 754
publisher
Portland Press Limited
external identifiers
  • pmid:15453829
  • wos:000226858300014
  • scopus:13444251163
ISSN
0264-6021
DOI
10.1042/BJ20041015
language
English
LU publication?
yes
id
5e3640e3-4f4a-4172-984a-0f5b81d02dee (old id 151122)
date added to LUP
2007-06-27 15:51:39
date last changed
2017-11-12 04:03:37
@article{5e3640e3-4f4a-4172-984a-0f5b81d02dee,
  abstract     = {Mediatorless, electrochemically driven, redox transformations of TI (type 1) and T2 copper sites in Trametes hirsuta laccase were studied by cyclic voltarnmetry and spectroclectrochernical redox titrations using bare gold electrode. DET (direct electron transfer) between I he 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 TI 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-potentiai laccases/oxiclases from totally different sources might be very similar, i.e. approx. 400 mV, is discussed.},
  author       = {Shleev, Sergey and Christenson, Andreas and Serezhenkov, V and Burbaev, D and Yaropolov, A and Gorton, Lo and Ruzgas, Tautgirdas},
  issn         = {0264-6021},
  language     = {eng},
  number       = {Part 3},
  pages        = {745--754},
  publisher    = {Portland Press Limited},
  series       = {Biochemical Journal},
  title        = {Electrochemical redox transformations of T1 and T2 copper sites in native Trametes hirsuta laccase at gold electrode},
  url          = {http://dx.doi.org/10.1042/BJ20041015},
  volume       = {385},
  year         = {2005},
}