Characterization of two new multiforms of Trametes pubescens laccase
(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:
https://lup.lub.lu.se/record/674328
- author
- Shleev, Sergey LU ; Nikitina, Oxana ; Christenson, Andreas LU ; Reimann, Curt LU ; Yaropolov, Alexander I. ; Ruzgas, Tautgirdas LU and Gorton, Lo LU
- organization
- publishing date
- 2007
- 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
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- 32fecca9-b66a-4dba-9dc8-dda5851cada3 (old id 674328)
- date added to LUP
- 2016-04-01 15:58:23
- date last changed
- 2022-03-22 07:32:47
@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}},
keywords = {{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}},
doi = {{10.1016/j.bioorg.2006.08.001}},
volume = {{35}},
year = {{2007}},
}