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Promoting laccase activity towards non-phenolic substrates: a mechanistic investigation with some laccase-mediator systems.
TLDR
Support to the conclusions is provided by investigating the intermolecular selectivity of oxidation with appropriate substrates, attempting Hammett correlations for the oxidation of a series of 4-X-substituted benzyl alcohols and measuring the kinetic isotope effect.
Mechanistic and steric issues in the oxidation of phenolic and non-phenolic compounds by laccase or laccase-mediator systems. The case of bifunctional substrates
TLDR
Experimental support is attained for the central role of laccase in biodelignification, in spite of the seemingly lower oxidation power of this enzyme with respect to other and stronger oxidising enzymes excreted by ligninolytic fungi.
An assessment of the relative contributions of redox and steric issues to laccase specificity towards putative substrates.
TLDR
The efficiency of oxidation was found to increase with the decrease in redox potential of the substrates, and the Marcus reorganisation energy for electron transfer to the T1 copper site was determined.
Chemical messengers: mediated oxidations with the enzyme laccase
TLDR
Experimental evidence is provided that enables the radical hydrogen atom transfer route with the laccase/HBT, laccases/HPI and l Accase/VLA systems to be assessed unambiguously, although the lAccase/TEMPO system follows a different and ionic oxidation route.
New mediators for the enzyme laccase: mechanistic features and selectivity in the oxidation of non-phenolic substrates
New mediators of laccase have been comparatively evaluated and ranked towards the benchmark aerobic oxidation of p-MeO-benzyl alcohol. The mechanism of oxidation of this non-phenolic substrate by
Kinetics of oxidation of benzyl alcohols by the dication and radical cation of ABTS. Comparison with laccase-ABTS oxidations: an apparent paradox.
TLDR
It is alternatively suggested that degradation by-products of either ABTS++ or ABTS*+ are formed in situ by hydrolysis during the laccase-ABTS reactions, and may be responsible for the observed oxidation of non-phenolics.
How is the reactivity of laccase affected by single-point mutations? Engineering laccase for improved activity towards sterically demanding substrates
TLDR
A series of single-point mutants on the basis of the amino-acid layout inside the reducing substrate active site known from the crystal structure of the enzyme are designed to improve the oxidation ability of Trametes versicolor laccase towards bulky phenolic substrates.
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