4-Nitro 2-picoline-l-oxide complexes of lanthanide perchlorates

4-Nitro 2-picoline-l-oxide (NPicO) complexes of the formulae La (NPicO)5 (CIO4)3, Ln2 (NPicO)9 (C1O4)6 (Ln = Pr, Nd, and Gd) and Ln (NPicO)4 (CIO4)3 (Ln == Tb, Dy, Ho and Yb) have been synthesised and characterised by analysis, electrolytic conductance, infrared, proton NMR and electronic spectral data. A tentative coordination number of 6 for all the complexes have been assigned

Carbon-13 NMR studies of lipid mobilization pattern in germinating groundnut (Arachis hypogaea L.) seeds

The products of lipid mobilization in groundnut (Arachis hypogaea L.) seeds as a function of time immediately after imbibition are monitored by 13C NMR. Different parts of the embryonic axis, namely,the radicle, hypocotyl, and plumule, exhibit characteristic time dependent 13C NMR spectra observed at 24-h intervals after imbibition. The various stages in the transformation of storage lipids present in different parts of the embryonic axis are clearly demonstrated. The transformaton of storage lipids is completed first in the radicle followed by the hypocotyl and finally the plumule. A mechanism of the transformation of the storage lipids is discussed.

Radical Annulation Strategy to Chiral Pupukeanones: Total Synthesis of (+)-10-ex&l(- Naphthyl)pupukean-9-onea nd (+)-lO-exo-l(- Naphthyl)-5-epipupukean-9-ones1

Intramolecular alkylation reaction of the bromoenone 12, obtained from S-carvone in three steps, furnished the bicyclo[2.2.2]octenone 13. Contrary to the anticipated radical annulation reaction, the bicyclic bromides 14 and 15, obtained from the enone 13, generated exclusively the cyclopropane product 18 via a 3-exo-trig radical cyclization on reaction with nBu3SnH and AIBN, even in the presence of a large excess of a radicophile. On the other hand, bromoenone 24, synthesized from R-carvone via S-naphthylcarvone 21, underwent radical annulation reaction in the presence of radicophiles to furnish the isotwistanes 25-28 in a regio- and stereospecific manner. Hydrogenation of the olefin 34, obtained from the diketone 27 via a regiospecific Wittig reaction, furnished the naphthyl-5-epipupukean-9-one 33, whereas stereoselective hydrogenation of the enone 36, prepared from the keto ester 25 via a Grignard reaction and dehydration sequence, generated the naphthylpupukeanone 32.

Squeezed states, photon-number distributions, and U(l) invariance

We study the photon-number distribution in squeezed states of a single-mode radiation field. A U(l)-invariant squeezing criterion is compared and contrasted with a more restrictive criterion, with the help of suggestive geometric representations. The U(l) invariance of the photon-number distribution in a squeezed coherent state, with arbitrary complex squeeze and displacement parameters, is explicitly demonstrated. The behavior of the photon-number distribution for a representative value of the displacement and various values of the squeeze parameter is numerically investigated. A new kind of giant oscillation riding as an envelope over more rapid oscillations in this distribution is demonstrated.

Stereochemical properties and x-ray structure of a water-soluble diastereomeric (arene)ruthenium(II) Schiff-base complex: [Ru(.eta.-MeC6H4Pri-p)(H2O)(L*)](ClO4), containing a weakly bound aqua ligand [HL* = (S)-(.alpha.-methylbenzyl)salicylaldimine]

An air-stable and water-soluble diastereomeric half-sandwich ruthenium(I1) complex, [Ru(s-MeCsH4Pr'-p)(H*O)-(L*)] (C104) (l), has been isolated and structurally characterized [HL* = (27)-(a methylbenzyl)salicylaldimine,2-HOC6H4CH-NCHMePhI. Complex 1, Czd-I3oNO&lRu, crystallizes in the noncentric triclinic space group P1 with a = 9.885(1) A, b = 10.185(1) A, c = 14.187(2) A, a = 110.32(1)', 6 = 102.17(1)', y = 102.41(1)O, V=1243( 1) A3, and 2 = 2. The X-ray structure shows the presence of two diastereomers in a 1:l ratio having RR,,,SCand SR,,,&c onfigurations. The Ru-OHz bond distances are considerably long, and the values for RR, - a~n d SRu-1isomers are 2.1 19(5) and 2.203(5) A, respectively. The aqua complex (1) exists as a single diastereomer in solution,and it forms stable adducts with P-, N-, and halide-donor ligands. The stereochemical changes associated with adduct-forming reactions follow an inversion order: PPhs >> P(OMe)3 > pyridine bases >> halides (I, Br, Cl) >H20.

A new quinone from Maesa indica (Roxb)A DC, (Myrsinaceae)

Isolation and structure elucidation of kiritiquinone, a new benzoquinone 2 5 dihydroxy-6-methyl 3 (hemeos 16-enyl)-1 4 benzoquinone from the frutis of Masca indica (Roxb) A DC is described

A regiospecific radical annulation strategy to functionalised chiral bicyclo[3.3.l]nonanes

A radical annulation, i.e. an intermolecular radical Michael addition followed by an intramolecular Michael addition of the resultant radical (radical cyclisation) has been employed for the construction of chiral functionalised bicyclo[3.3,1]-nonanes. Thus reaction of carvone hydrohalides 7 with (n)Bu(3)SnH and AIBN in the presence of excess of radicophiles 4 furnished, regiospecifically bicyclo[3.3.1]nonanes 8-14, introducing three new chiral centres in a stereoselective manner. Analogously the bromide 18 generated the bridgehead substituted bicyclo[3.3.1]-nonanes 19-21.

Chloroplastic glutamine synthetase from normal and water stressed safflower (Carthamus tinctorius L.) leaves

The chloroplastic isoform of glutamine synthetase (GS(2), EC 6.3.1.2) from normal and water stressed safflower (Carthamus tinctorius L. cv.A-300) leaves has been purified to apparent electrophoretic homogeneity by a procedure involving anion-exchange, hydrophobic and size-exclusion chromatography followed by electroelution of the protein from preparative polyacrylamide gels. The observed molecular weight of the native protein varied from 305-330 kDa depending on the sizing column employed. The native protein is composed of 44 kDa subunits. Under conditions of saturating ammonium and at ATP levels of 0.1-10 mM, double-reciprocal plots with respect to glutamate are biphasic and concave downward at high concentrations of the varied substrate for normal enzyme but are linear for enzyme from water-stressed plants. Under subsaturating ATP levels, K-Glu is over 18-fold lower for enzyme from stressed leaves. The K-m, (ATP) varies with Mg2+ levels in the assay mixture. Double-reciprocal plots of initial velocity with respect to ATP at changing fixed levels of NH4+ are linear for normal enzyme but are curved upwards for enzyme from stressed leaves. Initial velocity data of 1/v vs. 1/ammonium for the enzyme from both the sources are non-linear (curved upwards) when ATP is saturating. At subsaturating ATP levels, the data are linear for normal enzyme but are still non-linear for the enzyme from stressed leaves. The results obtained suggest positively cooperative binding of NH4+ A V-max(/2) value of 3.6 mM for Mg2+ was obtained at 5 mM ATP. The isoelectric point of the native protein from normal and stressed leaves was determined to be, respectively, 5.6 and 6.1. The mixed competitive and competitive inhibitors, methionine sulfoximine and ADP and K-i values of 0.086 mM (0.017 for the enzyme from stressed leaves) and 2.15 mM (1.70 for the enzyme from stressed leaves), respectively. Enzyme from stressed leaves is not inhibited by 5 mM proline. The observed kinetic constants of GS(2) from normal and water stressed safflower seedlings are discussed in relation to the known water-stress tolerance of this crop plant.

Interaction of EcoP1 modification methylase with S-adenosyl-L-methionine: a UV-crosslinking study

EcoP1 modification methylase was radioactively labeled when incubated with S-adenosyl-L-[methyl-3H]methionine in the presence of ultraviolet light. Crosslinking of the enzyme as detected by electrophoresis on sodium dodecyl sulfate-polyacrylamide gel followed by fluorography and autoradiography, was shown to be specific by a number of criteria. More importantly, EcoP1 modification methylase was also radioactively labeled with S-adenosyl-L-[carboxyl-14C]methionine demonstrating that labeling involved binding of the entire AdoMet molecule rather than methylation of the protein. Further, c2 EcoP1 mutant DNA modification methylases which show negligible or very little methylation activity, correspondingly formed a weak or no adduct upon crosslinking. These results suggest that photolabeling of EcoP1 DNA modification methylase occurs at the AdoMet binding site.

Interactions of L-serine at the active site of serine hydroxymethyltransferases: induction of thermal stability

Serine hydroxymethyltransferase (SHMT), EC 2.1.2.1, exhibits broad substrate and reaction specificity. In addition to cleaving many 3-hydroxyamino acids to glycine and an aldehyde, the enzyme also catalyzed the decarboxylation, transamination and racemization of several substrate analogues of amino acids. To elucidate the mechanism of interaction of substrates, especially L-serine with the enzyme, a comparative study of interaction of L-serine with the enzyme from sheep liver and Escherichia coli, was carried out. The heat stability of both the enzymes was enhanced in the presence of serine, although to different extents. Thermal denaturation monitored by spectral changes indicated an alteration in the apparent T, of sheep liver and E. coli SHMTs from 55 +/- 1 degrees C to 72 +/- 3 degrees C at 40 mM serine and from 67 +/- 1 degrees C to 72 +/- 1 degrees C at 20 mM serine, respectively. Using stopped flow spectrophotometry k values of (49 +/- 5)(.)10(-3) s(-1) and (69 +/- 7).10(-3) s(-1) for sheep liver and E. coli enzymes were determined at 50 mM serine. The binding of serine monitored by intrinsic fluorescence and sedimentation velocity measurements indicated that there was no generalized change in the structure of both proteins. However, visible CD measurements indicated a change in the asymmetric environment of pyridoxal 5'-phosphate at the active site upon binding of serine to both the enzymes. The formation of an external aldimine was accompanied by a change in the secondary structure of the enzymes monitored by far UV-CD spectra. Titration microcalorimetric studies in the presence of serine (8 mM) also demonstrated a single class of binding and the conformational changes accompanying the binding of serine to the enzyme resulted in a more compact structure leading to increased thermal stability of the enzyme.