Glyoxylates

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Oliver Reiser - One of the best experts on this subject based on the ideXlab platform.

Adiyala Vidyasagar - One of the best experts on this subject based on the ideXlab platform.

B N Sivasankar - One of the best experts on this subject based on the ideXlab platform.

  • spectral thermal and x ray studies on some new bis hydrazine lanthanide iii Glyoxylates
    Journal of Thermal Analysis and Calorimetry, 2008
    Co-Authors: B Raju, B N Sivasankar
    Abstract:

    Some new and bis-hydrazine lanthanide Glyoxylates Ln[OOC-CHO]3(N2H4)2 where Ln=La, Ce, Pr, Nd, Sm, Eu, Gd, Tb or Dy have been prepared and the compositions of the complexes have been determined by chemical analysis and elemental analysis. The magnetic moment and electronic spectra suggest except Ln3+ which is diamagnetic and all the other complexes are paramagnetic. Infrared spectral data indicate the bidentate coordination of carboxylates group is coordinate to lanthanide ion in a monodentate fashion. However, as a whole, glyoxylate ion acts as a bidentate ligand. The curves of all the complexes show multi-step degradation and the final products are found to be the respective metal oxides. The final residues were identified by their metal analysis, infrared spectra and the X-ray powder diffraction patterns. X-ray powder patterns of the complexes are almost super-imposable as expected which is in favour of isomorphism among the series.

  • spectral thermal and x ray studies on some new bis hydrazine metal Glyoxylates and bis hydrazine mixed metal Glyoxylates
    Thermochimica Acta, 2007
    Co-Authors: L Vikram, B N Sivasankar
    Abstract:

    Abstract Bis-hydrazine complexes of metal Glyoxylates and mixed metal Glyoxylates of 3d-metal ions of the formula M(OOCCHO) 2 (N 2 H 4 ) 2 , where M = Mg, Mn, Co, Ni, Cu, Zn or Cd and M 1/3 Co 2/3 (OOCCHO) 2 (N 2 H 4 ) 2 , where M = Mg, Mn, Ni, Zn or Cd, respectively, have been prepared and studied. The compositions of the complexes have been determined by chemical analyses. The magnetic moments and electronic spectra suggest a high-spin octahedral geometry for the metal complexes. Infrared spectral data indicate the bidentate bridging by hydrazine molecules and monodentate coordination by glyoxylate ions in both the metal and mixed metal compounds. Thermogravimetry and differential thermal analyses in air have been used to study the thermal behaviour of the complexes. The simultaneous TG-DTA traces of all the complexes show multi-step degradation and the final products are found to be the respective metal oxides in the case of metal complexes and metal cobaltites in the case of mixed metal complexes. The final residues were identified by their X-ray powder diffraction patterns. X-ray powder diffraction patterns of the complexes including mixed metal complexes are almost superimposable with in each of the series indicating isomorphism. The metal cobaltites MCo 2 O 4 , where M = Mg, Mn, Ni, Zn or Cd were also prepared by decomposing the respective mixed metal complex in a pre-heated silica crucible at about 300 °C, and their identities were confirmed by chemical analyses, infrared spectra and X-ray powder diffraction.

Leszek A. Kleczkowski - One of the best experts on this subject based on the ideXlab platform.

  • The Enzymic Reduction of Glyoxylate and Hydroxypyruvate in Leaves of Higher Plants
    Plant physiology, 1992
    Co-Authors: Curtis V. Givan, Leszek A. Kleczkowski
    Abstract:

    Glyoxylate and hydroxypyruvate are metabolites involved in the pathway of carbon in photorespiration. The chief glyoxylate-reducing enzyme in leaves is now known to be a cytosolic glyoxylate reductase that uses NADPH as the preferred cofactor but can also use NADH. Glyoxylate reductase has been isolated from spinach leaves, purified to homogeneity, and characterized kinetically and structurally. Chloroplasts contain lower levels of glyoxylate reductase activity supported by both NADPH and NADH, but it is not yet known whether a single chloroplastic enzyme catalyzes glyoxylate reduction with both cofactors. The major hydroxypyruvate reductase activity of leaves has long been known to be a highly active enzyme located in peroxisomes; it uses NADH as the preferred cofactor. To a lesser extent, NADPH can also be used by the peroxisomal enzyme. A second hydroxypyruvate reductase enzyme is located in the cytosol; it preferentially uses NADPH but can also use NADH as cofactor. In a barley mutant deficient in peroxisomal hydroxypyruvate reductase, the NADPH-preferring cytosolic form of the enzyme permits sufficient rates of hydroxypyruvate reduction to support continued substrate flow through the terminal stages of the photosynthetic carbon oxidation (glycolate/glycerate) pathway. The properties and metabolic significance of the cytosolic and organelle-localized glyoxylate and hydroxypyruvate reductase enzymes are discussed.

Peter Kreitmeier - One of the best experts on this subject based on the ideXlab platform.