37 resultados para aerobic

em Indian Institute of Science - Bangalore - Índia


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DURING recent years, there has been increasing amount of evidence regarding the importance of protozoa in the aerobic purification of sewage1–4 and, more recently, some quantitative observations on protozoa in determining the condition of sludge and quality of effluent have been recorded5–10. The evidence so far obtained has, however, been only indirect, chiefly owing to the difficulty in separating the protozoa from the associated bacteria. This has now been achieved and the object of this note is to show that the isolated protozoa can bring about practically all the changes associated with the purification. The part played by the bacteria is almost negligible.

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Epoxidation of alkenes by molecular oxygen is effected in high yields by catalysis of RuCl2(biox)(2) using isobutyraldehyde as the co-reductant: the reaction is stereospecific and regioselective.

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A solvent-free synthesis of alpha-aminonitriles and beta-nitroamines by oxidative cross-dehydrogenative coupling under aerobic condition is reported. A catalytic amount of molybdenum(VI) acetylacetonoate was found to catalyze cyanation of tertiary amines to form alpha-aminonitriles, whereas vanadium pentoxide was found to promote aza-Henry reaction to furnish beta-nitroamines. Both of these environmentally benign reactions are performed in the absence of solvents using molecular oxygen as an oxidant.

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Molybdenum trioxide (MoO3) catalyzed efficient oxidative cross-dehydrogenative-coupling (CDC) method for C-H functionalization of N-aryl tetrahydroisoquinolines has been explored. This user-friendly method of synthesizing alpha-aminophosphonates employs 1.1 equiv of dialkyl-H-phosphonate under aerobic condition. Formation of new C-P bonds from unfunctionalized starting materials under environmentally benign conditions provides an excellent avenue for the synthesis of biologically active alpha-aminophosphonates. (C) 2012 Elsevier Ltd. All rights reserved.

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A chemoselective reduction of olefins and acetylenes is demonstrated by employing catalytic amounts of ferric chloride hexahydrate (FeCl3 center dot 6H(2)O) and aqueous hydrazine (NH2NH2 center dot H2O) as hydrogen source at room temperature. The reduction is chemoselective and tolerates a variety of reducible functional groups. Unlike other metal-catalysed reduction methods, the present method employs a minimum amount of aqueous hydrazine (1.5-2 equiv.). Also, the scope of this method is demonstrated in the synthesis of ibuprofen in aqueous medium.

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An efficient aerobic reduction of olefins, internal as well as terminal, is developed using guanidine as an organocatalyst. A remarkable chemoselectivity in reduction has been demonstrated in the presence of a variety of functional groups and protective groups and a selective reduction of a terminal olefin in the presence of an internal olefin is revealed.

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A versatile aerobic catalytic system (I-2 and O-2/TBHP) for C-H functionalization is reported. This CDC (cross-dehydrogentive coupling) reaction is compatible with a large number of nucleophiles and is performed under ambient reaction conditions. The scope of the metal-free CDC is illustrated by synthesizing a variety of functionalized tetrahydroisoquinolines and N,N-dimethylaniline. The highlight of the method is a Friedel-Crafts reaction of phenols and indole with tertiary amines.

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Reaction of cobalt(II) perchlorate hexahydrate with a potentially tetradentate Schiff base ligand, HL (2-methoxy-6-(2-diethylaminoethylimino)methyl]phenol) in presence of sodium azide and sodium thiocyanate yields two complexes Co( L)( HL)(N-3)]center dot ClO4 ( 1) and Co( L)( HL)(NCS)] center dot ClO4 ( 2); both being characterized by different physicochemical methods. Crystal structure of 1 was determined by single crystal X-ray diffraction while that of 2 was reported earlier. In 1, the central cobalt(III) adopts slightly distorted octahedral geometry with same donor set to that of 2. Catalytic efficacy of the complexes towards epoxidation of different alkenes under aerobic condition were investigated in homogeneous medium which reveals that 1 is better catalyst than 2 with respect to alkene oxidation, reflected from the turn over frequencies (TOF) measured at an optimum temperature of 60 degrees C in acetonitrile. (C) 2014 Published by Elsevier B.V.

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Mycobacterium tuberculosis genes Rv0844c/Rv0845 encoding the NarL response regulator and NarS histidine kinase are hypothesized to constitute a two-component system involved in the regulation of nitrate metabolism. However, there is no experimental evidence to support this. In this study, we established M. tuberculosis NarL/NarS as a functional two-component system and identified His(241) and Asp(61) as conserved phosphorylation sites in NarS and NarL, respectively. Transcriptional profiling between M. tuberculosis H37Rv and Delta narL mutant strain during exponential growth in broth cultures with or without nitrate defined an similar to 30-gene NarL regulon that exhibited significant overlap with DevR-regulated genes, thereby implicating a role for the DevR response regulator in the regulation of nitrate metabolism. Notably, expression analysis of a subset of genes common to NarL and DevR regulons in M. tuberculosis Delta devR, Delta devS Delta dosT, and Delta narL mutant strains revealed that in response to nitrite produced during aerobic nitrate metabolism, the DevRS/DosT regulatory system plays a primary role that is augmented by NarL. Specifically, NarL itself was unable to bind to the narK2, acg, and Rv3130c promoters in phosphorylated or unphosphorylated form; however, its interaction with DevR similar to P resulted in cooperative binding, thereby enabling co-regulation of these genes. These findings support the role of physiologically derived nitrite as a metabolic signal in mycobacteria. We propose NarL-DevR binding, possibly as a heterodimer, as a novel mechanism for co-regulation of gene expression by the DevRS/DosT and NarL/NarS regulatory systems.

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Knowledge of the generation of H202 in cellular oxidations has existed for many years. It has been assumed that H202 is tOxiC tO cells and the presence of catalase is indicative of a detoxication mechanism. Other radicals of oxygen were recently recognized to be more potent destructive agents of biological material than H202. Also catalase and other peroxidases utilize H202 in some cellular oxidation processes leading to several important metabolites. Thus, the generation of H202 in cellular processes seems to be purposeful and H202 can not be dismissed as a mere undesirable byproduct. Biological formation of H202 is not limited to the previously known flavoproteins and some copper enzymes, but other redox systems, particularly heme and non-heme iron proteins, are now found to undergo auto-oxidation yielding H202. The capacity for generation of H202 is now found to be widespread in a variety of organisms and in the organdies of the cells. The reduction of oxygen to H20 by mitochondrial cytochrome oxidase being the predominant oxygen-utilizing reaction had over-shadowed the importance of the quantitatively minor pathways. Under aerobic conditions generation of H202 by a Variety of biomembranes has now been found to be a physiological event interlinked with phenomena such as phagocytosis, transport processes and thermogenesis in some as yet unidentified way. The underlying mechanisms of these processes seem to involve generation and utilization of H202 in mitochondria, microsomes, peroxisomes or plasma membranes. This review gives an account of the potential of biomembranes to generate H202 and its implication in the cellular processes.

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Thiobacillus ferrooxidans oxidized the sulphide minerals e.g., pyrite, pyrrhotite and copper concentrate under anaerobic conditions in the presence of ferric ion as sole electron acceptor. Copper and iron were solubilized from sulphide ores by the sulphur (sulphide)-dependent ferric-ion oxidoreductase activity. Treatment of resting cells of T. ferrooxidans with 0.5% phenol for 30 min completely destroyed the iron- and copper-solubilizing activity. The above treatment destroyed the sulphur(sulphide)-dependent ferric-ion-reducing activity completely but did not affect the iron-oxidizing activity. The results suggest that sulphur(sulphide)-dependent ferric-ion-reducing activity actively participates in the oxidation of sulphide minerals under anaerobic conditions. The activity of sulphur(sulphide)-dependent ferric ion reduction in the solubilization of iron and copper from the sulphide ores were also observed under aerobic conditions in presence of sodium azide (0.1 μmol), which completely inhibits the iron-oxidizing activity.

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Sun salutation is a part of yoga. It consists of a sequence of postures done with synchronized breathing. The practice of few cycles of sun salutation is known to help in maintaining good health and vigor. The practice of sun salutation does not need any extra gadgets. Also it is very much aerobic and invigorates the body and the mind.

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Cobalt(III) complexes [Co(pnt)(B)(2)](NO3)(2) (1-3) of pyridine-2-thiol (pnt) and phenanthroline bases (B), viz. 1,10-phenanthroline (phen in 1), dipyrido[3,2-d: 2',3'-f]quinoxaline (dpq in 2) and dipyrido[3,2-a:2',3'-c] phenazine (dppz in 3), have been prepared, characterized and their photo-induced anaerobic DNA cleavage activity studied. The crystal structure of 1a as mixed ClO4- and PF6- salt of 1 shows a (CoN5S)-N-III coordination geometry in which the pnt and phen showed N,S- and N,N-donor binding modes, respectively. The complexes exhibit Co(III)/Co(II) redox couple near -0.3 V (vs. SCE) in 20% DMF-Tris-HCl buffer having 0.1 M TBAP. The complexes show binding propensity to calf thymus DNA giving K-b values within 2.2 x 10(4)-7.3 x 10(5) M-1. Thermal melting and viscosity data suggest DNA surface and/or groove binding of the complexes. The complexes show significant anaerobic DNA cleavage activity in red light under argon atmosphere possibly involving sulfide anion radical or thiyl radical species. The DNA cleavage reaction under aerobic medium in red light is found to involve both singlet oxygen and hydroxyl radical pathways. The dppz complex 3 shows non-specific BSA and lysozyme protein cleavage activity in UV-A light of 365 nm via both hydroxyl and singlet oxygen pathways. The dppz complex 3 exhibits photocytotoxicity in HeLa cervical cancer cells giving IC50 values of 767 nM and 19.38 mu M in UV-A light of 365 nm and in the dark, respectively. A significant reduction of the dark toxicity of the dppz base (IC50 = 8.34 mu M in dark) is observed on binding to the cobalt(III) center.