4 research outputs found
Organocatalyzed Epoxidation of Alkenes in Continuous Flow using a Multi-Jet Oscillating Disk Reactor
CATALYTIC PROCESS FOR THE PREPARATION OF HYDROPEROXIDES OF ALKYLBENZENES BY AEROBIC OXIDATION UNDER MILD CONDITIONS
The present invention relates to a catalytic process for the preparation of hydroperoxides of alkylbenzenes by means of aerobic oxidation under mild conditions. More specifically, the present invention relates to a new catalytic process, which is significantly improved respect to the known art, for the aerobic oxidation in liquid phase of alkylbenzenes to hydroperoxide, industrially used for the preparation of styrene, propylene oxide, diphenols and ketones
Glyoxalase II promotes "in vitro" S-glutathionylation.
S-glutathionylation involves the reversible formation of a mix disulphide-bridge between specific cysteine and a molecule of glutathione, the major non-protein antioxidant compound in the cell. Mechanisms of protein S-glutathionylation are far to be completely understood and several reactions can promote it, either spontaneously or catalyzed. For the first time Glo II enzyme was studied as a new potential candidate to promote S-glutathionylation. To demonstrate its active involvement in protein glutathionylation were used actin, malate dehydrogenase and GAPDH purified proteins, which are known to be glutathionylated, for in vitro experiments..This work shows active involvement of cytosolic Glo II for in vitro protein S-glutathionylation. To confirm the role of Glo II, preliminary protein-protein docking studies was performed between Glo II and human actin. The data showed a high propensity to aggregate with other proteins through its catalytic site Further, in silico investigation of Glo II stability and behavior, conducted through full atom molecular dynamics simulations, showed an high folding stability together with a great affinity towards its own reaction product glutathione both protonated (GSH) and unprotonated (GS(-)). These studies, revealed that GloII, using its natural substrate SLG, allow a rapid and specific protein-SSG formation, leading enzymatic regulation of S-glutathionylation in proteins of different origin and cellular compartmentalization