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

Stereocontrol in Preparation of Cyclopalladated Alkylaromatic Oximes and Evaluation of Their Stereoselective Esterase-Type Catalytic Activity

The stereochemistry of 2′-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>)-2′-methylbutyrophenone oxime (<b>1</b><i><b>S</b></i>) and (<i>R</i>)-2′-methylbutyrophenone oxime (<b>1</b><i><b>R</b></i>) were equal to 92 ± 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 Pd­(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