40 research outputs found
Structure of native laccase from Trametes hirsuta at 1.8 {\AA} resolution
This paper describes the structural analysis of the native form of laccase from Trametes hirsuta at 1.8 A resolution. This structure provides a basis for the elucidation of the mechanism of catalytic action of these ubiquitous proteins. The 1.8 A resolution native structure provided a good level of structural detail compared with many previously reported laccase structures. A brief comparison with the active sites of other laccases is given
Kinetic and theoretical comprehension of diverse rate laws and reactivity gaps in <em>Coriolus hirsutus </em>laccase-catalyzed oxidation of acido and cyclometalated Ru<sup>II </sup>complexes
Kinetic and Theoretical Comprehension of Diverse Rate Laws and Reactivity Gaps in Coriolus hirsutus
An ortho-palladated dimethylbenzylamine complex as a highly efficient turnover catalyst for the decomposition of PīS insecticides. Mechanistic studies of the methanolysis of some PīS-containing phosphorothioate triesters
Photoinduced Multielectron Transfer to a Multicopper Oxidase Resulting in Dioxygen Reduction into Water
Probing the Surface of a Laccase for Clues towards the Design of Chemo-Enzymatic Catalysts
Stereocontrol in Preparation of Cyclopalladated Alkylaromatic Oximes and Evaluation of Their Stereoselective Esterase-Type Catalytic Activity
The stereochemistry
of 2ā²-methylbutyrophenone oxime, the
rates of <i>ortho</i>-palladation of its <i>E</i>- and <i>Z</i>-isomers, and catalytic activity of the respective
Pd complexes were studied. The full stereoisomeric composition of
oximes was established for the first time by means of supercritical
fluid chromatography on chiral polysaccharide column. It was shown
that enantiomeric excesses of both <i>E</i>/<i>Z</i>-isomers of (<i>S</i>)-2ā²-methylbutyrophenone oxime
(<b>1</b><i><b>S</b></i>) and (<i>R</i>)-2ā²-methylbutyrophenone oxime (<b>1</b><i><b>R</b></i>) were equal to 92 Ā± 2. The cyclopalladation
study revealed that while <i>E</i>-isomer is <i>ortho</i>-palladated very quickly its <i>Z</i>-counterpart does
not enter this reaction. However, upon coordination to PdĀ(II), <i>Z</i>-oxime slowly isomerizes into <i>E</i>-form with
fast subsequent cyclopalladation, so it was possible to perform <i>ortho</i>-palladation of <i>E-</i>oxime in kinetic
resolution mode with removal of unreacted <i>Z</i>-oxime.
Comparatively rare <i>cis</i>-structure of cyclopalladated
oxime dimer was proved by means of single-crystal X-ray study. For
the first time, it was shown that <i>ortho</i>-palladated
chiral oximes behave as enantioselective catalyst in the hydrolysis
of chiral esters