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Characterization of two new multiforms of Trametes pubescens laccase

Shleev, Sergey LU ; Nikitina, Oxana; Christenson, Andreas LU ; Reimann, Curt LU ; Yaropolov, Alexander I.; Ruzgas, Tautgirdas LU and Gorton, Lo LU (2007) In Bioorganic Chemistry 35(1). p.35-49
Abstract
Electrochemical properties of two multiforms of laccase from Trametes pubescens basidiomycete (LACI and LAC2) have been studied. The standard redox potentials of the T1 sites of the enzymes were found to be 746 and 738 mV us. NHE for LACI and LAC2, respectively. Bioelectroreduction of oxygen based on direct electron transfer between each of the two forms of Trametes pubescens laccase and spectrographic graphite electrodes has been demonstrated and studied. It. is concluded that the T1 site of laccase is the first electron acceptor, both in solution (homogeneous case) and when the enzymes are adsorbed on the surface of the graphite electrode (heterogeneous case). Thus, the previously proposed mechanism of oxygen bioelectroreduction by... (More)
Electrochemical properties of two multiforms of laccase from Trametes pubescens basidiomycete (LACI and LAC2) have been studied. The standard redox potentials of the T1 sites of the enzymes were found to be 746 and 738 mV us. NHE for LACI and LAC2, respectively. Bioelectroreduction of oxygen based on direct electron transfer between each of the two forms of Trametes pubescens laccase and spectrographic graphite electrodes has been demonstrated and studied. It. is concluded that the T1 site of laccase is the first electron acceptor, both in solution (homogeneous case) and when the enzymes are adsorbed on the surface of the graphite electrode (heterogeneous case). Thus, the previously proposed mechanism of oxygen bioelectroreduction by adsorbed fungal laccase was additionally confirmed using two forms of the enzyme. Moreover, the assumed need for extracellular laccase to communicate directly and electronically with a solid matrix (lignin) in the course of lignin degradation is discussed. In summary, the possible roles of multiforms of the enzyme based on their electrochemical, biochemical, spectral, and kinetic properties have been suggested to consist in broadening of the substrate specificity of the enzyme, in turn yielding the possibility to dynamically regulate the process of lignin degradation according to the real-time survival needs of the organism. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
lignin, T1 site, redox potential, Trametes pubescens, laccase, degradation
in
Bioorganic Chemistry
volume
35
issue
1
pages
35 - 49
publisher
Elsevier
external identifiers
  • wos:000244378300004
  • scopus:33846252766
ISSN
0045-2068
DOI
10.1016/j.bioorg.2006.08.001
language
English
LU publication?
yes
id
32fecca9-b66a-4dba-9dc8-dda5851cada3 (old id 674328)
date added to LUP
2007-12-14 15:35:54
date last changed
2017-09-24 04:22:12
@article{32fecca9-b66a-4dba-9dc8-dda5851cada3,
  abstract     = {Electrochemical properties of two multiforms of laccase from Trametes pubescens basidiomycete (LACI and LAC2) have been studied. The standard redox potentials of the T1 sites of the enzymes were found to be 746 and 738 mV us. NHE for LACI and LAC2, respectively. Bioelectroreduction of oxygen based on direct electron transfer between each of the two forms of Trametes pubescens laccase and spectrographic graphite electrodes has been demonstrated and studied. It. is concluded that the T1 site of laccase is the first electron acceptor, both in solution (homogeneous case) and when the enzymes are adsorbed on the surface of the graphite electrode (heterogeneous case). Thus, the previously proposed mechanism of oxygen bioelectroreduction by adsorbed fungal laccase was additionally confirmed using two forms of the enzyme. Moreover, the assumed need for extracellular laccase to communicate directly and electronically with a solid matrix (lignin) in the course of lignin degradation is discussed. In summary, the possible roles of multiforms of the enzyme based on their electrochemical, biochemical, spectral, and kinetic properties have been suggested to consist in broadening of the substrate specificity of the enzyme, in turn yielding the possibility to dynamically regulate the process of lignin degradation according to the real-time survival needs of the organism.},
  author       = {Shleev, Sergey and Nikitina, Oxana and Christenson, Andreas and Reimann, Curt and Yaropolov, Alexander I. and Ruzgas, Tautgirdas and Gorton, Lo},
  issn         = {0045-2068},
  keyword      = {lignin,T1 site,redox potential,Trametes pubescens,laccase,degradation},
  language     = {eng},
  number       = {1},
  pages        = {35--49},
  publisher    = {Elsevier},
  series       = {Bioorganic Chemistry},
  title        = {Characterization of two new multiforms of Trametes pubescens laccase},
  url          = {http://dx.doi.org/10.1016/j.bioorg.2006.08.001},
  volume       = {35},
  year         = {2007},
}