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`Yellow' laccase of Panus tigrinus oxidizes non‐phenolic substrates without electron‐transfer mediators
It is supposed that yellow laccase is formed as a result of blue lAccase modification by products of lignin degradation, and these compounds might play a role of natural electron‐transfer mediators for the oxidation of non‐phenolic substances, catalyzed by yellow l Accase. Expand
Crystal structure of a blue laccase from Lentinus tigrinus: evidences for intermediates in the molecular oxygen reductive splitting by multicopper oxidases
This is the first structure of a multicopper oxidase which allowed the detection of two intermediates in the molecular oxygen reduction and splitting, providing general insights into the reductive cleavage of the O-O bonds, a leading problem in many areas of biology. Expand
Biotransformation of soil humic acids by blue laccase of Panus tigrinus 8/18: an in vitro study
Abstract We describe here the role of the polyphenoloxidases in the oxidation of recalcitrant soil organic compounds and consider what changes occur in their structure during experiments on theExpand
Degradation of 3,4‐Dichloro‐ and 3,4‐Difluoroaniline by Pseudomonas fluorescens 26‐K
3,4‐Dichloro‐ and 3, 4‐difluoroanilines were degraded by Pseudomonas fluorescens 26‐K under aerobic conditions and the presence of 3‐chloro‐4‐hydroxyaniline as a metabolite suggested that 3,4-DCA degradation pathway includes dehalogenation and hydroxylation of aromatic ring followed by its subsequent cleaving by C2,3DO. Expand
Blue and yellow laccases of ligninolytic fungi.
Comparison of N-terminal amino acid sequences of purified laccases showed high homology between blue and yellow-brown laccase forms, and Formation of yellow laccased as a result of binding of lignin-derived molecules by enzyme protein is proposed. Expand
New efficient producers of fungal laccases
The maximal laccase activity was observed in the case of submerged cultivation of the mycelium immobilized on polycaproamide fibers in rich media in the presence of 2 mM CuSO4 in combination with the optimal inducer, namely, 2,6-dimethylphenol for L. strigosus and 2,4-dimethylamine for S. ochraceum. Expand
Crystal Structure of the Hydroxyquinol 1,2-Dioxygenase from Nocardioides simplex 3E, a Key Enzyme Involved in Polychlorinated Aromatics Biodegradation*
The primary sequence determination and the analysis of the crystal structure of the 1,2-HQD from Nocardioides simplex 3E solved at 1.75 Å resolution are reported, the first structure of an intradiol dioxygenase specialized in hydroxyquinol ring cleavage to be investigated in detail. Expand
Characterization of a Protocatechuate Catabolic Gene Cluster from Rhodococcus opacus 1CP: Evidence for a Merged Enzyme with 4-Carboxymuconolactone-Decarboxylating and 3-Oxoadipate
A 3-oxoadipate enol-lactone-hydrolyzing enzyme, purified from benzoate-grown cells of Rhodococcus opacus (erythropolis) 1CP, was found to have a larger molecular mass under denaturing conditions than the corresponding enzymes previously purified from gamma-proteobacteria. Expand
A New Modified ortho Cleavage Pathway of 3-Chlorocatechol Degradation by Rhodococcus opacus 1CP: Genetic and Biochemical Evidence
UV overlay spectra as well as high-pressure liquid chromatography analyses confirmed that 2-chloro-cis,cis-muconate is transformed by ClcB2 to 5-chloromuconolactone, which during turnover byClcF gives cis-dienelactone as the sole product. Expand
Characterization of catechol catabolic genes from Rhodococcus erythropolis 1CP
Based on sequences of the N terminus and of tryptic peptides of the muconate cycloisomerase, a fragment of the corresponding gene has now been amplified and used as a probe for the cloning of catechol catabolic genes from R. erythropolis. Expand