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High Catalytic Efficiency (high + catalytic_efficiency)
Selected AbstractsChemInform Abstract: Tripeptides of the Type H-D-Pro-Pro-Xaa-NH2 as Catalysts for Asymmetric 1,4-Addition Reactions: Structural Requirements for High Catalytic Efficiency.CHEMINFORM, Issue 6 2010Markus Wiesner Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a "Full Text" option. The original article is trackable via the "References" option. [source] Tripeptides of the Type H- D -Pro-Pro-Xaa-NH2 as Catalysts for Asymmetric 1,4-Addition Reactions: Structural Requirements for High Catalytic EfficiencyCHEMISTRY - A EUROPEAN JOURNAL, Issue 39 2009Markus Wiesner Dr. Abstract Analysis of the structural and functional requirements within the asymmetric peptidic catalyst H- D -Pro-Pro-Asp-NH2 led to the development of the closely related peptide H- D -Pro-Pro-Glu-NH2 as an even more efficient catalyst for asymmetric conjugate addition reactions of aldehydes to nitroolefins. In the presence of as little as 1,mol,% of H- D -Pro-Pro-Glu-NH2, a broad range of aldehydes and nitroolefins react readily with each other. The resulting ,-nitroaldehydes were obtained in excellent yields and stereoselectivities at room temperature. Within the structure of the peptidic catalysts, the D -Pro-Pro motif is the major contributor to the high stereoselectivities. The C-terminal amide and the spacer to the carboxylic acid in the side-chain of the C-terminal amino acid are responsible for the fine-tuning of the stereoselectivity. The peptidic catalysts not only allow for highly effective asymmetric catalysis under mild conditions, but also function in the absence of additives. Die sorgfältige Analyse der strukturellen und funktionalen Erfordernisse des peptidischen Katalysators H- D -Pro-Pro-Asp-NH2 führte zur Entwicklung des verwandten Peptids H- D -Pro-Pro-Glu-NH2, das einen noch effizienteren Katalysator für asymmetrische konjugierte Additionsreaktionen von Aldehyden an Nitroolefine darstellt. In Gegenwart von nur 1,mol,% von H- D -Pro-Pro-Glu-NH2 reagiert eine große Auswahl verschiedenster Aldehyde und Nitroolefine unter milden Bedingungen bereitwillig miteinander. Die entstehenden ,-Nitroaldehyde bilden sich in exzellenten Ausbeuten und Stereoselektivitäten bei Raumtemperatur. Innerhalb der Struktur des peptidischen Katalysators trägt das D -Pro-Pro Motiv am meisten zu den hohen Stereoselektivitäten bei. Das C-terminale Amid und der Linker vom Peptidrückgrat zur Carbonsäure in der Seitenkette der C-terminalen Aminosäure sind für die Feineinstellung der Stereoselektivitäten verantwortlich. Die peptidischen Katalysatoren sind nicht nur höchst effiziente asymmetrische Katalysatoren sondern benötigen im Gegensatz zu vielen anderen chiralen Katalysatoren auch keine Additive für ihre katalytische Effizienz. [source] The role of group bulkiness in the catalytic activity of psychrophile cold-active protein tyrosine phosphataseFEBS JOURNAL, Issue 17 2008Hiroki Tsuruta The cold-active protein tyrosine phosphatase found in psychrophilic Shewanella species exhibits high catalytic efficiency at low temperatures as well as low thermostability, both of which are characteristics shared by many cold-active enzymes. The structure of cold-active protein tyrosine phosphatase is notable for the presence of three hydrophobic sites (termed the CA, Zn-1 and Zn-2 sites) behind the loop structures comprising the catalytic region. To identify the structural components responsible for specific enzyme characteristics, we determined the structure of wild-type cold-active protein tyrosine phosphatase at high resolution (1.1 Å) and measured the catalytic efficiencies of enzymes containing mutations in the three hydrophobic sites. The bulkiness of the amino acid side chains in the core region of the Zn-1 site strongly affects the thermostability and the catalytic efficiency at low temperatures. The mutant enzyme I115M possessed a higher kcat at low temperatures. Elucidation of the crystal structure of I115M at a resolution of 1.5 Å revealed that the loop structures involved in retaining the nucleophilic group and the acid catalyst are more flexible than in the wild-type enzyme. [source] Enhanced Photocatalytic Activity using Layer-by-Layer Electrospun Constructs for Water RemediationADVANCED FUNCTIONAL MATERIALS, Issue 15 2010Jung Ah Lee Abstract Endocrine disruptors such as bisphenol A (BPA) are environmental pollutants that interfere with the body's endocrine system because of their structural similarity to natural and synthetic hormones. Due to their strong oxidizing potential to decompose such organic pollutants, colloidal metal oxide photocatalysts have attracted increasing attention for water detoxification. However, achieving both long-term physical stability and high efficiency simultaneously with such photocatalytic systems poses many challenges. Here a layer-by-layer (LbL) deposition approach is reported for immobilizing TiO2 nanoparticles (NPs) on a porous support while maintaining a high catalytic efficiency for photochemical decomposition of BPA. Anatase TiO2 NPs ,7,nm in diameter self-assemble in consecutive layers with positively charged polyhedral oligomeric silsesquioxanes on a high surface area, porous electrospun polymer fiber mesh. The TiO2 LbL nanofibers decompose approximately 2.2,mg BPA per mg of TiO2 in 40,h of illumination (AM 1.5G illumination), maintaining first-order kinetics with a rate constant (k) of 0.15,h,1 for over 40,h. Although the colloidal TiO2 NPs initially show significantly higher photocatalytic activity (k,,,0.84,h,1), the rate constant drops to k,,,0.07,h,1 after 4,h of operation, seemingly due to particle agglomeration. In the BPA solution treated with the multilayered TiO2 nanofibers for 40,h, the estrogenic activity, based on human breast cancer cell proliferation, is significantly lower than that in the BPA solution treated with colloidal TiO2 NPs under the same conditions. This study demonstrates that water-based, electrostatic LbL deposition effectively immobilizes and stabilizes TiO2 NPs on electrospun polymer nanofibers for efficient extended photochemical water remediation. [source] Genetic and catalytic efficiency structure of an HCV protease quasispecies,HEPATOLOGY, Issue 4 2007Sandra Franco The HCV nonstructural protein (NS)3/4A serine protease is not only involved in viral polyprotein processing but also efficiently blocks the retinoic-acid,inducible gen I and Toll-like receptor 3 signaling pathways and contributes to virus persistence by enabling HCV to escape the interferon antiviral response. Therefore, the NS3/4A protease has emerged as an ideal target for the control of the disease and the development of new anti-HCV agents. Here, we analyzed, at a high resolution (approximately 100 individual clones), the HCV NS3 protease gene quasispecies from three infected individuals. Nucleotide heterogeneity of 49%, 84%, and 91% were identified, respectively, which created a dense net that linked different parts of the viral population. Minority variants having mutations involved in the acquisition of resistance to current NS3/4A protease inhibitors (PIs) were also found. A vast diversity of different catalytic efficiencies could be distinguished. Importantly, 67% of the analyzed enzymes displayed a detectable protease activity. Moreover, 35% of the minority individual variants showed similar or better catalytic efficiency than the master (most abundant) enzyme. Nevertheless, and in contrast to minority variants, master enzymes always displayed a high catalytic efficiency when different viral polyprotein cleavage sites were tested. Finally, genetic and catalytic efficiency differences were observed when the 3 quasispecies were compared, suggesting that different selective forces were acting in different infected individuals. Conclusion: The rugged HCV protease quasispecies landscape should be able to react to environmental changes that may threaten its survival. (HEPATOLOGY 2007;45:899,910.) [source] Prolylprolinol-Catalyzed Asymmetric Michael Addition of Aliphatic Aldehydes to NitroalkenesADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 4 2010Dengfu Lu Abstract Several novel prolylprolinol catalysts have been designed and synthesized. This type of compound showed high catalytic efficiency on promoting the direct addition of unmodified aldehydes to nitroalkenes. Among the catalysts surveyed, the least bulky member (8d) exhibited the best performance on both efficiency and stereoselectivity, providing the products with up to 97% ee value with 1.5,5,mol% catalyst loading. Additionally, computational studies of the transition state have been conducted to explain the high diastereo- and enantioselectivity. [source] Air-Stable and Highly Active Dendritic Phosphine Oxide- Stabilized Palladium Nanoparticles: Preparation, Characterization and Applications in the Carbon-Carbon Bond Formation and Hydrogenation ReactionsADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 6 2008Lei Wu Abstract Dendrimer-stabilized palladium nanoparticles were formed in the reduction of palldium bis(acetylacetonate) [Pd(acac)2] in the presence of phosphine dendrimer ligands using hydrogen in tetrahydrofuran. The resulting Pd nanoparticles were characterized by TEM, 31P,NMR and 31P MAS NMR. The results indicated that the dendritic phosphine ligands were oxidized to phosphine oxides. These dendrimer-stabilized Pd nanoparticles were demonstrated to be efficient catalysts for Suzuki and Stille coupling reactions and hydrogenations. The dendritic wedges served as a stabilizer for keeping the nanoparticles from aggregating, and as a vehicle for facilitating the separation and/or the recycling of the Pd catalyst. In the case of the Suzuki coupling reaction, these Pd nanoparticles exhibited high catalytic efficiency (TON up to 65,000) and air stability as compared with the commonly used homogeneous catalyst tetrakis(triphenylphosphine)palladium [Pd(PPh3)4]. In addition, the results obtained from the bulky dendritic substrate suggest that the Pd nanoparticles might act as reservoir of catalytically active species, and that the reaction is actually catalyzed by the soluble Pd(0) and/or Pd(II) species leached from the nanoparticle surface. [source] The structure of human deoxycytidine kinase in complex with clofarabine reveals key interactions for prodrug activationACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2006Yan Zhang Clofarabine [2-chloro-9-(2-deoxy-2-fluoro-,- d -arabinofuranosyl)-9H -purin-6-amine] is a hybrid of the widely used anticancer drugs cladribine and fludarabine. It is the precursor of an effective chemotherapeutic agent for leukemias and other hematological malignancies and received accelerated approval by the FDA for the treatment of pediatric patients with relapsed or refractory acute lymphoblastic leukemia. Clofarabine is phosphorylated intracellularly by human deoxycytidine kinase (dCK) to the 5,-monophosphate, which is the rate-limiting step in activation of the prodrug. dCK has a broad substrate specificity, with a much higher activity to deoxycytidine than to deoxyadenosine and deoxyguanosine. As a purine-nucleoside analog, clofarabine is a better substrate of dCK than deoxycytidine. The crystal structure of dCK has been solved previously in complex with pyrimidine nucleosides and ADP [Sabini et al. (2003), Nature Struct. Biol.10, 513,519]. In the current study, the crystal structure of clofarabine- and ADP-bound dCK was solved to 2.55,Å by molecular replacement. It appears that the enzyme takes the same conformation as in the structures of the pyrimidine nucleoside-bound complexes. The interactions between 2-Cl and its surrounding hydrophobic residues contribute to the high catalytic efficiency of dCK for clofarabine. [source] Expression, purification, crystallization and preliminary X-ray crystallographic studies of a psychrophilic cellulase from Pseudoalteromonas haloplanktisACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2003Sébastien Violot The Antarctic psychrophile Pseudoalteromonas haloplanktis produces a cold-active cellulase. To date, a three-dimensional structure of a psychrophilic cellulase has been lacking. Crystallographic studies of this cold-adapted enzyme have therefore been initiated in order to contribute to the understanding of the molecular basis of the cold adaptation and the high catalytic efficiency of the enzyme at low and moderate temperatures. The catalytic core domain of the psychrophilic cellulase CelG from P. haloplanktis has been expressed, purified and crystallized and a complete diffraction data set to 1.8,Å has been collected. The space group was found to be P212121, with unit-cell parameters a = 135.1, b = 78.4, c = 44.1,Å. A molecular-replacement solution, using the structure of the mesophilic counterpart Cel5A from Erwinia chrysanthemi as a search model, has been found. [source] Enzyme-Carrying Polymeric Nanofibers Prepared via Electrospinning for Use as Unique BiocatalystsBIOTECHNOLOGY PROGRESS, Issue 5 2002Hongfei Jia Improvement of catalytic efficiency of immobilized enzymes via materials engineering was demonstrated through the preparation of bioactive nanofibers. Bioactive polystyrene (PS) nanofibers with a typical diameter of 120 nm were prepared and examined for catalytic efficiency for biotransformations. The nanofibers were produced by electrospinning functionalized PS, followed by the chemical attachment of a model enzyme, ,-chymotrypsin. The observed enzyme loading as determined by active site titration was up to 1.4% (wt/wt), corresponding to over 27.4% monolayer coverage of the external surface of nanofibers. The apparent hydrolytic activity of the nanofibrous enzyme in aqueous solutions was over 65% of that of the native enzyme, indicating a high catalytic efficiency as compared to other forms of immobilized enzymes. Furthermore, nanofibrous ,-chymotrypsin exhibited a much-improved nonaqueous activity that was over 3 orders of magnitude higher than that of its native counterpart suspended in organic solvents including hexane and isooctane. It appeared that the covalent binding also improved the enzyme's stability against structural denaturation, such that the half-life of the nanofibrous enzyme in methanol was 18-fold longer than that of the native enzyme. [source] Synthesis and Structure of an Extremely Air-Stable Binuclear Hafnocene Perfluorooctanesulfonate Complex and Its Use in Lewis Acid-Catalyzed ReactionsCHEMISTRY - A EUROPEAN JOURNAL, Issue 26 2009Renhua Qiu Abstract Stable complexes: An extremely air-stable ,2 -hydroxy-bridged binuclear hafonocene perfluorooctanesulfoante complex shows high catalytic efficiency in Lewis acid-catalyzed reactions, such as esterification, Friedel,Crafts acylation, the Mukaiyama aldol reation, and the allylation of aldehyde (see scheme). An extremely air-stable ,2 -hydroxy-bridged binuclear hafonocene perfluorooctanesulfoante complex was successfully synthesized. This complex showed high catalytic efficiency in the esterification of alcohols, phenol, thiol, and amines, in the Friedel,Crafts acylation of alylaryl ethers, in the Mukaiyama aldol reaction, and in the allylation of aldehydes and could be reused. [source] | ||||||||||