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Autoreduction and aggregation of fungal laccase in solution phase: possible correlation with a resting form of laccase

Shleev, Sergey LU ; Reimann, Curt LU ; Serezhenkov, Vladimir ; Burbaev, Dosymzhan ; Yaropolov, Alexander ; Gorton, Lo LU and Ruzgas, Tautgirdas LU (2006) In Biochimie 88(9). p.1275-1285
Abstract
This paper reports results of a reexamination of some poorly understood peculiarities of laccases, an enzyme family which has been extensively studied in our laboratories as well as by others for some years. The issue that is reconsidered here is the previously proposed existence of ''active" and "resting" forms of laccases. The presence of fungal laccases with partly reduced active sites is demonstrated. Of further interest is that an aggregated state in solution, not to our knowledge previously noted for laccase, has been found by using small-angle X-ray scattering as well as thorough analysis of the results of several biochemical experiments. Under some conditions, this aggregated state may correlate with the resting form of the... (More)
This paper reports results of a reexamination of some poorly understood peculiarities of laccases, an enzyme family which has been extensively studied in our laboratories as well as by others for some years. The issue that is reconsidered here is the previously proposed existence of ''active" and "resting" forms of laccases. The presence of fungal laccases with partly reduced active sites is demonstrated. Of further interest is that an aggregated state in solution, not to our knowledge previously noted for laccase, has been found by using small-angle X-ray scattering as well as thorough analysis of the results of several biochemical experiments. Under some conditions, this aggregated state may correlate with the resting form of the laccases, although this resting form could have a broader significance. It was shown that Trametes ochracea laccase had some anomalous characteristics, which could be correlated with the high concentration of the "resting" enzyme. The mechanism of formation of resting laccase is suggested. Knowledge of the resting state is of importance for in vitro studies. Additionally, a suggestion about the possible regulatory role of this form in vivo is mentioned. (c) 2006 Elsevier SAS. All rights reserved. (Less)
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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
SAXS, EPR, T1 site, redox potential, fungi, laccase
in
Biochimie
volume
88
issue
9
pages
1275 - 1285
publisher
Elsevier
external identifiers
  • wos:000241481000018
  • scopus:33748796883
  • pmid:16581176
ISSN
1638-6183
DOI
10.1016/j.biochi.2006.02.007
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
6d0df18a-1938-47a9-a924-3ddb20abb731 (old id 387159)
date added to LUP
2016-04-01 12:22:12
date last changed
2021-09-22 04:30:45
@article{6d0df18a-1938-47a9-a924-3ddb20abb731,
  abstract     = {This paper reports results of a reexamination of some poorly understood peculiarities of laccases, an enzyme family which has been extensively studied in our laboratories as well as by others for some years. The issue that is reconsidered here is the previously proposed existence of ''active" and "resting" forms of laccases. The presence of fungal laccases with partly reduced active sites is demonstrated. Of further interest is that an aggregated state in solution, not to our knowledge previously noted for laccase, has been found by using small-angle X-ray scattering as well as thorough analysis of the results of several biochemical experiments. Under some conditions, this aggregated state may correlate with the resting form of the laccases, although this resting form could have a broader significance. It was shown that Trametes ochracea laccase had some anomalous characteristics, which could be correlated with the high concentration of the "resting" enzyme. The mechanism of formation of resting laccase is suggested. Knowledge of the resting state is of importance for in vitro studies. Additionally, a suggestion about the possible regulatory role of this form in vivo is mentioned. (c) 2006 Elsevier SAS. All rights reserved.},
  author       = {Shleev, Sergey and Reimann, Curt and Serezhenkov, Vladimir and Burbaev, Dosymzhan and Yaropolov, Alexander and Gorton, Lo and Ruzgas, Tautgirdas},
  issn         = {1638-6183},
  language     = {eng},
  number       = {9},
  pages        = {1275--1285},
  publisher    = {Elsevier},
  series       = {Biochimie},
  title        = {Autoreduction and aggregation of fungal laccase in solution phase: possible correlation with a resting form of laccase},
  url          = {http://dx.doi.org/10.1016/j.biochi.2006.02.007},
  doi          = {10.1016/j.biochi.2006.02.007},
  volume       = {88},
  year         = {2006},
}