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Electrochemistry and kinetics of fungal laccase mediators

Shumakovich, G. P. ; Shleev, Sergey LU ; Morozova, O. V. ; Khohlov, P. S. ; Gazaryan, I. G. and Yaropolov, A. I. (2006) In Bioelectrochemistry 69(1). p.16-24
Abstract
The screening of potential redox mediators for laccase was performed using homogeneous Trametes hirsuta laccase. Heterogeneous (electrochemical) and homogeneous (oxidation by laccase) reactions of the different types of the enhancers (mediators) of the enzyme were investigated. It was discovered that derivatives of phenyl-methyl-pyrazolones and benzoic acid, as well as N-hydroxynaphthalimide were efficient substrates for the laccase. The characterization of several representatives from each class was carried out using electrochemical and enzyme kinetics methods. The kinetic parameters for the oxidation of phenyl-methyl-pyrazolones and 3-(6-hylroxy)-aminobenzoic acid were comparable to those for... (More)
The screening of potential redox mediators for laccase was performed using homogeneous Trametes hirsuta laccase. Heterogeneous (electrochemical) and homogeneous (oxidation by laccase) reactions of the different types of the enhancers (mediators) of the enzyme were investigated. It was discovered that derivatives of phenyl-methyl-pyrazolones and benzoic acid, as well as N-hydroxynaphthalimide were efficient substrates for the laccase. The characterization of several representatives from each class was carried out using electrochemical and enzyme kinetics methods. The kinetic parameters for the oxidation of phenyl-methyl-pyrazolones and 3-(6-hylroxy)-aminobenzoic acid were comparable to those for 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) oxidation by the laccase, whereas the rate of enzymatic oxidation of N-hydroxynaphthalimide was sufficiently lower. Electrochemical experiments demonstrated that only oxidation of phenyl-methyl-pyrazolones and N-hydroxynaphthalimide yielded several high-potential intermediates capable of oxidizing veratryl alcohol, which was used as a lignin model substrate, whereas derivatives of benzoic acid showed low-potential intermediate, which was not able to oxidized lignin model compound. Phenyl-methyl-pyrazolones was about 50% as effective in degrading veratryl alcohol compared to ABTS as judged from HPLC kinetic studies, whereas N-hydroxynaphthalimide showed the same efficiency as ABTS. Phenyl-methyl-pyrazolones and hydroxynaphthalimides may be of commercial interest for oxidoreductase-catalyzed biodegradation of different xenobiotics. (c) 2005 Elsevier B.V. All rights reserved. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
benzoic acid, phenyl-methyl-pyrazolone, enhancer, laccase, mediator, hydroxynaphthalimide
in
Bioelectrochemistry
volume
69
issue
1
pages
16 - 24
publisher
Elsevier
external identifiers
  • pmid:16318928
  • wos:000240907600003
  • scopus:33747828439
  • pmid:16318928
ISSN
1878-562X
DOI
10.1016/j.bioelechem.2005.10.001
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
584dd115-8973-4dd9-9e0c-705150939c7f (old id 389771)
date added to LUP
2016-04-01 12:26:17
date last changed
2021-02-17 02:42:00
@article{584dd115-8973-4dd9-9e0c-705150939c7f,
  abstract     = {The screening of potential redox mediators for laccase was performed using homogeneous Trametes hirsuta laccase. Heterogeneous (electrochemical) and homogeneous (oxidation by laccase) reactions of the different types of the enhancers (mediators) of the enzyme were investigated. It was discovered that derivatives of phenyl-methyl-pyrazolones and benzoic acid, as well as N-hydroxynaphthalimide were efficient substrates for the laccase. The characterization of several representatives from each class was carried out using electrochemical and enzyme kinetics methods. The kinetic parameters for the oxidation of phenyl-methyl-pyrazolones and 3-(6-hylroxy)-aminobenzoic acid were comparable to those for 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) oxidation by the laccase, whereas the rate of enzymatic oxidation of N-hydroxynaphthalimide was sufficiently lower. Electrochemical experiments demonstrated that only oxidation of phenyl-methyl-pyrazolones and N-hydroxynaphthalimide yielded several high-potential intermediates capable of oxidizing veratryl alcohol, which was used as a lignin model substrate, whereas derivatives of benzoic acid showed low-potential intermediate, which was not able to oxidized lignin model compound. Phenyl-methyl-pyrazolones was about 50% as effective in degrading veratryl alcohol compared to ABTS as judged from HPLC kinetic studies, whereas N-hydroxynaphthalimide showed the same efficiency as ABTS. Phenyl-methyl-pyrazolones and hydroxynaphthalimides may be of commercial interest for oxidoreductase-catalyzed biodegradation of different xenobiotics. (c) 2005 Elsevier B.V. All rights reserved.},
  author       = {Shumakovich, G. P. and Shleev, Sergey and Morozova, O. V. and Khohlov, P. S. and Gazaryan, I. G. and Yaropolov, A. I.},
  issn         = {1878-562X},
  language     = {eng},
  number       = {1},
  pages        = {16--24},
  publisher    = {Elsevier},
  series       = {Bioelectrochemistry},
  title        = {Electrochemistry and kinetics of fungal laccase mediators},
  url          = {http://dx.doi.org/10.1016/j.bioelechem.2005.10.001},
  doi          = {10.1016/j.bioelechem.2005.10.001},
  volume       = {69},
  year         = {2006},
}