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showing 10 items of 184 documents
Cops and robbers: putative evolution of copper oxygen-binding proteins.
2000
Two closely related copper proteins, phenoloxidase and haemocyanin, are known to be involved in different physiological functions such as the primary immune response and oxygen transport. Although the proteins differ structurally, they have the same active site by which dioxygen is bound. Recent results reveal that haemocyanin also exhibits phenoloxidase activity. A scenario is proposed for the evolutionary relationships among copper oxygen-binding proteins (COPs).
Multi-Alkenylsilsesquioxanes as Comonomers and Active Species Modifiers of Metallocene Catalyst in Copolymerization with Ethylene.
2018
The copolymers of ethylene (E) with open-caged iso-butyl-substituted tri-alkenyl-silsesquioxanes (POSS-6-3 and POSS-10-3) and phenyl-substituted tetra-alkenyl-silsesquioxane (POSS-10-4) were synthesized by copolymerization over the ansa-metallocene catalyst. The influence of the kind of silsesquioxane and of the copolymerization conditions on the reaction performance and on the properties of the copolymers was studied. In the case of copolymerization of E/POSS-6-3, the positive comonomer effect was observed, which was associated with the influence of POSS-6-3 on transformation of the bimetallic ion pair to the active catalytic species. Functionality of silsesquioxanes and polymerization par…
The roles for a Lewis base and MgCl2 in third-generation Ziegler-Natta catalysts
1998
Activity of a titanium catalyst supported on a bimetallic magnesium-aluminium system, involving a Lewis base [MgCl2(THF) 2 /Al(C 2 H 5 ) 2 Cl], was studied in ethylene polymerization, and the effect of the catalyst composition on the properties of the final polymer produced was investigated. Analysis and discussion of the findings covering also some part of the kinetic study, resulted in defining the roles for MgCl 2 and a Lewis base in the third-generation Ziegler-Natta catalysts. MgCl 2 forms a bimetallic complex with an organoaluminium compound, which involves also a Lewis base. Its reaction with TiCl 4 yields a very active catalyst wherein the Mg: Ti molar ratio is close to 1. This mean…
Application of 3-Quinolinoyl Picket Porphyrins to the Electroreduction of Dioxygen to Water: Mimicking the Active Site of Cytochromec Oxidase
2001
International audience
Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale DFT/MM Methods
2020
<p>We present a detailed theoretical analysis of the reaction mechanism of proteolysis catalyzed by the main protease of SARS-CoV-2. Using multiscale simulation methods, we have characterized the interactions stablished by a peptidic substrate in the active site and then we have explored the free energy landscape associated to the acylation and de-acylation steps of the proteolysis reaction, characterizing the transition states of the process. Our mechanistic proposals can explain most of the experimental observations made on the highly similar ortholog protease of SARS-CoV. We point out to some key interactions that may facilitate the acylation process and thus can be crucial in the …
Optimization of peptidomimetic boronates bearing a P3 bicyclic scaffold as proteasome inhibitors
2014
Abstract A new series of pseudopeptide boronate proteasome inhibitors (2–3) was developed, through optimization of our previously described analogs of bortezomib, bearing a bicyclic 1,6-naphthyridin-5(6H)-one scaffold as P3 fragment (1). The biological evaluation on human 20S proteasome displayed a promising inhibition profile, especially for compounds bearing a P2 ethylene fragment, which exhibited Ki values in the nanomolar range for the ChT-L activity (e.g. 2a, Ki = 0.057 μM) and considerable selectivity for proteasome over bovine pancreatic α-chymotrypsin. Docking experiments into the yeast 20S proteasome revealed that the ligands are accommodated predominantly into the ChT-L site and t…
The Recent Crystal Structure of Human Tyrosinase Related Protein 1 (HsTYRP1) Solves an Old Problem and Poses a New One
2017
Show your metal: l-Tyrosine is converted into the protective antioxidative polymer melanin in a sequence of reactions. In humans, the catalytic pathway starts with the tyrosinase HsTYR and two tyrosinase-related proteins HsTYRP1 and HsTYRP2. All three enzymes have the same active site but the latter two contain two zinc ions instead of copper ions.
Structural properties, conformational stability and oxygen binding properties of Penaeus monodon hemocyanin
2004
Hemocyanin sequences allineament shows the presence of highly invariant regions especially in the active site and in the tight intersubunits interaction sites. Comparing the aminoacids in contact regions between monomers is possible to interpret the stability of hexamers.
Conversion of crustacean hemocyanin to catecholoxidase
2004
Crustacean hemocyanin as oxygen carrier and catecholoxidase as enzymes belong to the same protein family (type 3 copper proteins) sharing very similar active sites. Treatment with SDS of these hemocyanins results in an opening of the entrance to the active site for bulky phenolic compounds. This demonstrates, that almost all hemocyanin subunits possess the ability of catecholoxidase activity.
Unraveling the SARS-CoV-2 Main Protease Mechanism Using Multiscale Methods
2020
We present a detailed theoretical analysis of the reaction mechanism of proteolysis catalyzed by the main protease of SARS-CoV-2. Using multiscale simulation methods, we have characterized the interactions established by a peptidic substrate in the active site, and then we have explored the free energy landscape associated with the acylation and deacylation steps of the proteolysis reaction, characterizing the transition states of the process. Our mechanistic proposals can explain most of the experimental observations made on the highly similar ortholog protease of SARS-CoV. We point to some key interactions that may facilitate the acylation process and thus can be crucial in the design of …