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Journal ArticleDOI

Mixed metal complexes of iron-molybdenum with 8-quinolinolate and dithiocarbamates

TL;DR: In this paper, the authors have shown that the complexes are nonelectrolytes in dimethylformamide and are in the III and V oxidation states, respectively, with octahedral geometry around each atom.
Abstract: Iron-molybdenum heterometallic complexes, FeMoO2R4-(H2O) (R=8-quinolinolate, diethyldithiocarbamate, 4-morpholinyl-dithiocarbamate and piperidinyldithiocarbamate), have been prepared from iron(III) molybdate. T.l.c. and x-ray diffraction studies indicate that the complexes are discrete species. The complexes are non-electrolytes in dimethylformamide. Magnetic measurements suggest that the iron and molybdenum are in the III and V oxidation states, respectively, with octahedral geometry around each atom. I.r. spectral studies indicate the presence of MoO3+ and FeOMo bridges and the monoionic bidentate nature of the ligands. Electronic spectral and thermal decomposition studies on these complexes are reported.
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Journal ArticleDOI
TL;DR: The authors present des travaux concernant la preparation, the structure moleculaire, the caracterisation spectrometrique et la reactivite de complexes de metaux de transition avec des coordinats carboxyliques, heterocycliques, polyamines ou aldimines.

72 citations

References
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Journal ArticleDOI
TL;DR: In this paper, the infra-red absorption spectra of solid 8-hydroxyquinoline, 2-methyl-8-hydroxynoline, 4-methyl 8-hexynoline and a number of metal chelates derived from these reagents were studied.

168 citations

Book ChapterDOI
01 Jan 1983
TL;DR: In this paper, the authors have shown that the enzyme nitrogenase contains two metal-sulfur clusters: the iron-molybdenum cofactor (FeMo-co), which contains one Mo, 6−7 Fe, and ∼ 4 S atoms in a spincoupled paramagnetic (S=3/2) cluster; and the P clusters, variants of normal but highly reduced 4 Fe-4 S clusters in which three Fe atoms are somehow distinguished from the fourth and which, when oxidized, exhibit an usually high spin (S = 5/
Abstract: Studies on the enzyme nitrogenase have shown that it contains two novel metal-sulfur clusters: the iron-molybdenum cofactor (FeMo-co), which contains one Mo, 6–7 Fe, and ∼ 4 S atoms in a spincoupled paramagnetic (S=3/2) cluster; and the P clusters, variants of normal but highly reduced 4 Fe-4 S clusters in which three Fe atoms are somehow distinguished from the fourth and which, when oxidized, exhibit an usually high spin (S=5/2 or 7/2) ground state. No structures consistent with all available spectroscopic data have been proposed for either unit. Synthetic efforts aimed at developing models for FeMo-co have utilized tetrathiomolybdate as starting material, and have resulted in two well-characterized classes of Mo-Fe-S cluster: those containing the MoFe3S4 “cubane” core and those containing a “linear” MoS2Fe unit. The former apparently contain Mo in a relatively reduced valence state (ca. + 3) and exhibit Mo-S and Mo-Fe distances in good agreement with those found for the Mo site of nitrogenase; the latter contain Mo in a higher oxidation state (ca. + 6) and have significantly shorter Mo-S distances. Synthetic work related to the P clusters has centered on the properties of the [Fe4S4(SR)4]3− ions, for which two different structures with different magnetic properties are found, and on the properties of 4 Fe-4 S clusters with non-thiolate ligands.

42 citations

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