Enzymatic oxidation of manganese ions catalysed by laccase

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Enzymatic oxidation of manganese ions catalysed by laccase

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Publication Article, peer reviewed scientific
Title Enzymatic oxidation of manganese ions catalysed by laccase
Author(s) Shleev, Sergey
Date 2009
English abstract
Electrochemical properties of two multiforms of laccase from Trametes pubescens basidiomycete (LAC1 and LAC2) have been studied. The standard redox potentials of the T1 sites of the enzymes were found to be 746 and 738 mV vs. NHE for LAC1 and LAC2, respectively. Bioelectroreduction of oxygen based on direct electron transfer between each of 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.
DOI http://dx.doi.org/10.1016/j.bioorg.2006.08.001 (link to publisher's fulltext)
Publisher Elsevier Inc.
Host/Issue Bioorganic Chemistry;35
Volume 1
ISSN 0045-2068
Pages 35-49
Language eng (iso)
Subject(s) Laccase
Redox potential
Research Subject Categories::NATURAL SCIENCES
Handle http://hdl.handle.net/2043/8558 (link to this page)

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