Home About us Contact
|
Home About us Contact | ||
|
|
||
Low Catalytic Activity (low + catalytic_activity)
Selected AbstractsTransition metal complexes of a cyclic pseudo hexapeptide: synthesis, complex formation and catalytic activities,,JOURNAL OF PEPTIDE SCIENCE, Issue 9 2008Huong Ngyen Abstract To contribute to a better understanding of metalloenzymes, we studied ion selectivity, complex formation tendencies and catalytic activities of linear and cyclic pseudopeptides. In this contribution, a linear and cyclic pseudo hexapeptide is described. The complex with transition metal ions and the sequence were designed using the programme COSMOS. Different routes of solid-phase synthesis were performed and compared using anchoring by C -terminus or a His side chain, using preformed pseudodipeptide building units or formation of N -functionalized peptide bond during stepwise assembly. The different strategies were compared regarding cyclization tendency, yield and purity. Side-chain anchoring to solid support favours the cyclization but leads to the formation of difficult to separate dioxopiperazine. Both routes require preformed building units. Complex-formation tendencies and selectivity for certain bivalent transition metal ions were experimentally estimated and compared to ones predicted theoretically. CD measurements indicate conformational changes by complex formation with different metal ions. Catalytic activities on oxidation of catechol and hydrolysis of bis-phosphate esters by some metal complexes of linear and cyclic peptide show only low catalytic activities compared to other model peptides and related metalloenzymes. The preference of the cyclic peptide for complexation of Ni2+ corresponds well to the predictions of COSMOS-NMR force field calculations. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd. [source] New Bis(mercaptoimidazolyl)(pyrazolyl)borate Ligands and Their Zinc Complex ChemistryEUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 13 2003Mouhai Shu Abstract Nine new tripodal NS2 ligands of the bis(mercaptoimidazolyl)(pyrazolyl)borate type with varying 3-R-mercaptoimidazolyl moieties were prepared as their potassium salts. Treatment with zinc salts yielded the complex types L·Zn,Cl, L·Zn,I, L·Zn,ONO2, L·Zn,OClO3 and [L·Zn(imidazole)]ClO4. Attempts at the formation of L·Zn,OH or cationic L·Zn complexes resulted in dismutation and formation of ZnL2 complexes. Hydrolytic destruction yielded one [OZn4(thiooimidazolate)6] complex. The ZnS2NO coordination which is present in the enzyme-substrate complex of alcohol dehydrogenase could be successfully modelled by an [L·Zn(C2H5OH)]+ complex. The L·Zn,X complexes showed very low catalytic activity in the dehydrogenation of 2-propanol or the hydrogenation of p -nitrobenzaldehyde. The new compounds were identified by a total of 12 structure determinations. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003) [source] Studies of Pyridinyl-Containing 14-Membered Macrocyclic Copper(II) ComplexesEUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 7 2003Sabrina Autzen Abstract Six copper(II) complexes of tetracoordinating, pyridinyl-containing 14-membered macrocycles with varying ratios of nitrogen and oxygen donor atoms were prepared and characterized by IR, UV/Vis, and EPR spectroscopy and cyclic voltammetry. A distorted tetragonal coordination of the copper center in the solid-state was established by X-ray crystallography for the tetraazamacrocyclic complex Cu-3 carrying a methoxybenzyl pendent arm and the trioxaaza complex Cu-6. The superoxide dismutase-like activity of the CuII complexes was investigated by inhibition of NADH oxidation. Although the UV/Vis and EPR spectra of the complexes were strongly affected when the coordinating nitrogen atoms were successively replaced by oxygen atoms, no significant change in their reactivity towards superoxide was observed. In all cases a 1:1 or 1:2 stoichiometry for the reaction with superoxide was found, with the exception of the methoxybenzyl-substituted tetraaza complex, which showed a low catalytic activity with a turnover number of about 10. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003) [source] Structural and mutational analysis of TenA protein (HP1287) from the Helicobacter pylori thiamin salvage pathway , evidence of a different substrate specificityFEBS JOURNAL, Issue 21 2009Nicola Barison HP1287 (tenA) from Helicobacter pylori is included among the genes that play a relevant role in bacterium colonization and persistence. The gene has been cloned and its product, protein TenA, has been expressed and purified. The crystal structures of the wild-type protein and the mutant F47Y have been determined at resolutions of 2.7 and 2.4 Å, respectively. The molecular model, a homotetramer with 222 symmetry, shows that the H. pylori TenA structure belongs to the thiaminase II class of proteins. These enzymes were recently found to be involved in a salvage pathway for the synthesis of the thiamin precursor hydroxypyrimidine, which constitutes a building block in thiamin biosynthesis, in particular in bacteria living in the soil. By contrast, enzymatic measurements on TenA from H. pylori indicate that the activity on the putative substrate 4-amino-5-aminomethyl-2-methylpyrimidine is very modest. Moreover, in the present study, we demonstrate that the mutation at residue 47, a position where a phenylalanine occurs in all the strains of H. pylori sequenced to date, is not sufficient to explain the very low catalytic activity toward the expected substrate. As a result of differences in the colonization environment of H. pylori as well as the TenA structural and catalytic peculiar features, we suggest a possible pivotal role for the H. pylori enzyme in the thiamin biosynthetic route, which is in agreement with the relevance of this protein in the stomach colonization process. Structured digital abstract ,,MINT-7260232: TenA (uniprotkb:O25874) and TenA (uniprotkb:O25874) bind (MI:0407) by x-ray crystallography (MI:0114) [source] Performance study of heptane reforming in the dense ceramic membrane reactorsAICHE JOURNAL, Issue 1 2008Wenliang Zhu Abstract Heptane reforming was investigated in three dense ceramic membrane reactors, where the membranes were modified differently with reforming catalyst. Each reactor displayed distinctive catalytic behavior. The reactor with a bare membrane showed low catalytic activity and low oxygen permeation flux (JO2), but gave stable performance. The left two membranes reactors modified with catalyst both displayed shift processes at the preliminary stage of membrane reaction, not only in JO2 but also in the selectivity of all products. Moreover, the membrane reactor with more catalyst gave higher performance in the case of JO2 and CO selectivity. The observed shift phenomena are due to the activation of catalyst on the membrane surface, and the different amounts of catalyst produce different impaction on the membrane reactions. On the basis of the results in three membrane reactors, a reaction pathway of hydrocarbon reforming in dense ceramic membrane reactor is proposed. Being some different from combustion and reforming mechanism (CRR), hydrocarbon reforming in dense ceramic membrane reactor has its own characteristics. © 2007 American Institute of Chemical Engineers AIChE J, 2007 [source] Factor IX mutants with enhanced catalytic activityJOURNAL OF THROMBOSIS AND HAEMOSTASIS, Issue 10 2009R. HARTMANN Summary.,Background:,Activated coagulation factor IX (FIXa) has low catalytic activity towards its physiologic substrate FX when activated FVIII (FVIIIa) is absent. One reason for this is that the FIX surface loop 99 stabilizes FIXa in a conformation that limits access of FX to the active site. Objectives:,To investigate the effect of mutations in loop 99 and in the active site on FIXa activity with and without FVIIIa. Methods:,Five full-length FIX mutants with amino acid exchanges in the catalytic domain of FIX were constructed and characterized by measuring their activity in FX activation in model systems and in plasma. Results and Conclusions:,The mutants showed no or marginally improved catalytic properties in FX activation by the intrinsic tenase complex (FIXa,FVIIIa,Ca2+,phospholipid). The combination of mutations Y94F and K98T hardly affected FX activation in the presence of FVIIIa, but yielded a FIX molecule that, in FIX-depleted plasma, had , 2.5-fold higher clotting activity and , 3.5-fold higher activity in a thrombin generation assay than plasma-derived FIX (pdFIX). Two FIXa mutants had considerably increased activities towards FX in the absence of FVIIIa. FIXa-Y94F/K98T/Y177F/I213V/E219G (FIXa-L) and FIXa-Y94F/A95aK/K98T/Y177F/I213V/E219G (FIXa-M) activated FX with catalytic efficiencies (kcat/Km) that, as compared with activated pdFIX, were increased 17-fold and six-fold, respectively. However, in plasma, their zymogen forms performed similarly to pdFIX. This indicates that the introduced mutations not only affected the activity of FIXa but may have also influenced the lifetime of the activated mutant molecules in plasma by modifying their activation and/or inhibition rates. [source] Preliminary X-ray crystallographic studies of BthTX-II, a myotoxic Asp49-phospholipase A2 with low catalytic activity from Bothrops jararacussu venomACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2006L. C. Corrêa For the first time, a complete X-ray diffraction data set has been collected from a myotoxic Asp49-phospholipase A2 (Asp49-PLA2) with low catalytic activity (BthTX-II from Bothrops jararacussu venom) and a molecular-replacement solution has been obtained with a dimer in the asymmetric unit. The quaternary structure of BthTX-II resembles the myotoxin Asp49-PLA2 PrTX-III (piratoxin III from B. pirajai venom) and all non-catalytic and myotoxic dimeric Lys49-PLA2s. In contrast, the oligomeric structure of BthTX-II is different from the highly catalytic and non-myotoxic BthA-I (acidic PLA2 from B. jararacussu). Thus, comparison between these structures should add insight into the catalytic and myotoxic activities of bothropic PLA2s. [source] Bifunctional Heterogeneous Catalysis of Silica,Alumina-Supported Tertiary Amines with Controlled Acid,Base Interactions for Efficient 1,4-Addition ReactionsCHEMISTRY - A EUROPEAN JOURNAL, Issue 41 2009Ken Motokura Dr. Abstract We report the first tunable bifunctional surface of silica,alumina-supported tertiary amines (SA,NEt2) active for catalytic 1,4-addition reactions of nitroalkanes and thiols to electron-deficient alkenes. The 1,4-addition reaction of nitroalkanes to electron-deficient alkenes is one of the most useful carbon,carbon bond-forming reactions and applicable toward a wide range of organic syntheses. The reaction between nitroethane and methyl vinyl ketone scarcely proceeded with either SA or homogeneous amines, and a mixture of SA and amines showed very low catalytic activity. In addition, undesirable side reactions occurred in the case of a strong base like sodium ethoxide employed as a catalytic reagent. Only the present SA-supported amine (SA,NEt2) catalyst enabled selective formation of a double-alkylated product without promotions of side reactions such as an intramolecular cyclization reaction. The heterogeneous SA,NEt2 catalyst was easily recovered from the reaction mixture by simple filtration and reusable with retention of its catalytic activity and selectivity. Furthermore, the SA,NEt2 catalyst system was applicable to the addition reaction of other nitroalkanes and thiols to various electron-deficient alkenes. The solid-state magic-angle spinning (MAS) NMR spectroscopic analyses, including variable-contact-time 13C cross-polarization (CP)/MAS NMR spectroscopy, revealed that acid,base interactions between surface acid sites and immobilized amines can be controlled by pretreatment of SA at different temperatures. The catalytic activities for these addition reactions were strongly affected by the surface acid,base interactions. [source] | ||||||||||