Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Vanadium”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 73 records · Page 4Linked to original sources
PubMed1993

Microchromatographic analysis of lipids, protein, and occurrence of lipid peroxidation in various brain areas of vanadium exposed rats: a possible mechanism of vanadium neurotoxicity.

Administration of sodium metavanadate (3 mg/kg) to adult female Sprague Dawley rats for 5 consecutive days by intreaeritoneal route resulted in major alterations in lipid profiles and protein concentration in all the brain regions. Sodium metavanadate exposure displayed phospholipids, cholesterol and cerebrosides, and protein, but ganglioside concentration was significantly increased in various areas of the brain. Loss of body weight observed in this study could be attributed to the loss of appetite; loss of nutrients and wasting of tissues. It is likely that large amount of body water was lost through diarrhoea. Gas liquid chromatography has revealed that oleic acid, linoleic acid, linolenic acid, and archidonic acid were preferentially lost in the brain of vanadium-exposed rats. Thin layer chromatography further proved degradation of individual lipids. Sphingomyelin was substantially decreased followed by phosphatidyl choline and phosphatidyl ethanolamine, but phosphatidyl serine and phosphatidyl inositol were slightly affected. Our recent work has demonstrated vanadium-induced stimulation of lipid peroxidation in the various regions of the rat brain. It is speculative that deterioration of myelin sheath by vanadium exposure contributed to preferential lipid loss but lesser loss of protein. These studies also indicate that vanadium-induced stimulation of lipid peroxidation is characterized by a selective loss of brain polyunsaturated fatty acids and thus comprehensive degradation of lipids in the different regions of the rat brain. However, the mechanism involved in the elevation of ganglioside levels is not yet fully understood. It is concluded that these perturbations produced damage to the associated physiological functions leading to CNS dysfunctions.

Animals↗
PubMed2004

pH-specific synthesis of a dinuclear vanadium(V)-peroxo-citrate complex in aqueous solutions: pH-dependent linkage, spectroscopic and structural correlations with other aqueous vanadium(V)-peroxo-citrate and non-peroxo species.

Aqueous reactions of V2O5 or VCl3 in the presence of the physiological citric acid and hydrogen peroxide, in a pH specific fashion, afforded a new vanadium(V)-peroxo-citrate material isolated in a pure crystalline form. Elemental analysis pointed to the molecular formulation (NH4)6[V(V)2O2(O2)2(C6H4O7)2].4.5H2O (1). Complex 1 was further characterized by UV-vis, FT-IR, and X-ray crystallography. Compound 1 crystallizes in the monoclinic space group C2/c with a = 12.391(5) A, b = 15.737(7) A, c = 17.102(7) A, beta = 110.84(1) degrees, V = 3117(1) A3, and Z = 4. The structure of the anionic assembly consists of a planar V(V)2O2 core with two fully deprotonated citrates bound to it through the central carboxylate and alkoxide moieties as well as one of the terminal carboxylate groups. The presence of one peroxide group attached to each vanadium(V) renders the geometry around each metal center pentagonal bipyramidal. Key structural and spectroscopic features of 1 correlate with those seen in the peroxo congener and low-pH analogue (NH4)2[V(V)2O2(O2)2(C6H6O7)2].2H2O (3), in which all terminal carboxylate groups are protonated. In solution, simple pH-dependent transformation of 1 to 3 attests to their participation in the requisite speciation and potentiates the presence of other similar peroxo analogues not yet isolated and characterized. The reactivity of 1 through transformation reactions, yielding a plethora of well-characterized species, establishes a linkage among various species with the same or different vanadium oxidation states. Collectively, the data reflect soluble forms of vanadium with peroxide and citrate that contribute to the requisite pH-dependent distribution of that metal ion and likely influence biological processes.

Journal Article↗
PubMed1990

Iron K-edge X-ray-absorption spectroscopy of the iron-vanadium cofactor of the vanadium nitrogenase from Azotobacter chroococcum.

Iron K-edge e.x.a.f.s. data for the iron-vanadium cofactor (FeVaco) from Azotobacter chroococcum vanadium nitrogenase reported here provide further evidence for the structural similarity between this and the iron-molybdenum nitrogenase cofactor (FeMoco) from Klebsiella pneumoniae molybdenum nitrogenase [Arber, Flood, Garner, Gormal, Hasnain & Smith (1988) Biochem. J. 252, 421-425]. The e.x.a.f.s. data are consistent with the vanadium being present in a V-Fe-S cluster, thus confirming that the N-methylformamide extract of the VFe protein component of A. chroococcum vanadium nitrogenase does indeed contain a polynuclear metal-sulphur cluster. Additionally, a long Fe-Fe distance is observed as 0.369 nm, demonstrating the presence of a long-range order in the cluster.

Azotobacter↗
PubMed1982

Antimicrobial, insect sterilizing and ovicidal activity of some oxo-vanadium(IV) and oxo-vanadium(V) complexes.

Twenty-three newly synthesized mixed-ligand complexes of oxo-vanadium(IV) and oxo-vanadium(V) were studied for antimicrobial activity. Eight of these complexes were found to have microbicidal properties. The complexes [NH4][VO(gl)2]H2O (gl-H2 = glycolic acid) and [VO(ACOAP)(acac-H)]H20 (ACOAP-H2=Schiff base of acetylacetone and orthoaminophenol, acac-H=acetyl-acetone) show broad bactericidal spectra, while the complexes [VO(ACSAM)2]OH (ACSAM-H = Schiff base of acetylacetone and sulphanilamide) and [VO(CSSAM-H)2]H2O (CSSAM-H =Schiff base of 3-carboxy salicylaldehyde and sulphanilamide) possess pronounced antidermatophytic properties. The latter is inhibitory to plant pathogenic fungi as well. Plant tumour producing Agrobacterium tumefaciens is effectively inhibited in vitro by the complex [VO(ACTSC-Na)(acac)]H2O (ACTSC-H2 = condensation product of acetylacetone and thiosemicarbazide). Minimum inhibitory concentrations of all the active complexes are within the values of 0.125-2.00 mg/ml. Out of the 7 active complexes tested for 50% inhibition of conidial germination of Helminthosporium oryzae, a rice plant pathogen, only 1 complex, viz. [VO(acac) (ACACAACD)] (ACACAACD(H)NH4 equal Schiff base of acetylacetone and ammonium 2-amino-1-cyclopentene-1-dithiocarboxylate) shows a positive result. The effective concentration is 0.55 mg/ml. Three vanadium complexes were tested for insect sterilant and ovicidal properties on the red cotton bug, Dysdercus koenigi. The complex [VO(HASA-Na) (acac)]H2O (HASA-H2 = Schiff base of orthohydroxyacetophenone and anthr anilic acid) was found to be a suitable male sterilant.

Animals↗
PubMed1992

Desferrioxamine enhances the reactivity of vanadium (IV) and vanadium (V) toward ferri- and ferrocytochrome c.

Ligands, especially desferrioxamine, affect the rate at which vanadium reduces or oxidizes cytochrome c. Whether reduction or oxidation occurs, and how fast, depends on the nature of the ligand, the state of reduction of the vanadium, the pH (6.0, 7.0, or 7.4), and the availability of oxygen. In general, oxidation of ferrocytochrome c was favored by (1) low pH, (2) an oxidized state of the vanadium, (3) the presence of oxygen, and (4) more strongly binding ligands (desferrioxamine much greater than histidine = ATP greater than EDTA greater than albumin greater than aquo). Thus, at pH 6.0, desferrioxamine accelerated the V(V)-catalyzed ferrocytochrome c oxidation 160-fold aerobically, and 3500-fold anaerobically. In general, strongly binding ligands slowed oxidations, especially at higher pH. Desferrioxamine was unique among the five ligands in that it not only accelerated oxidation of ferrocytochrome c at pH 6.0, but at pH 7.4 the redox balance shifted to the point where it paradoxically reduced ferricytochrome c. V(V) is an improbable electron donor, but desferrioxamine will reduce cytochrome c, and V(V) accelerates this process. Oxidation of cytochrome c by V(V):desferrioxamine was faster anaerobically, and reduction by V(IV):desferrioxamine was faster aerobically. Although V(V) did not oxidize ferrocytochrome c at pH 7.4, V(IV) did, provided oxygen and desferrioxamine were both present. V(IV):desferrioxamine almost completely reduced ferricytochrome c, and this reduction was followed by a slow, progressive oxidation. This latter oxidation of cytochrome c is mediated by active species generated in the reaction between V(IV):desferrioxamine and oxygen, because none of these reagents alone can induce oxidation at a comparable rate. The mediating species were transient, and generated in reactions with oxygen.(ABSTRACT TRUNCATED AT 250 WORDS)

Catalase↗
PubMed2005

Influences of permeation of vanadium ions through PVDF-g-PSSA membranes on performances of vanadium redox flow batteries.

The preparation and physical characterization of a poly(vinylidene fluoride)-graft-poly(styrene sulfonic acid) (PVDF-g-PSSA) membrane prepared by a solution-grafting method were described. These membranes exhibited high conductivity with a value 3.22 x 10(-2) S/cm at 30 degrees C. ICP studies revealed that the PVDF-g-PSSA membrane showed dramatically lower vanadium ion permeability compared to Nafion 117. Trivalent vanadium ions had the highest permeability through all these membranes in contrast to pentavalent vanadium ions with the lowest. The VRB with the low-cost PVDF-g-PSSA membrane exhibited a higher performance than that with Nafion 117 under the same operating conditions, and its energy efficiency reached 75.8% at 30 mA/cm(2). The performance of VRB with the PVDF-g-PSSA membrane can be maintained after more than 200 cycles at a current density of 60 mA/cm(2).

Journal Article↗
PubMed1994

Vanadium activates or inhibits receptor and non-receptor protein tyrosine kinases in cell-free experiments, depending on its oxidation state. Possible role of endogenous vanadium in controlling cellular protein tyrosine kinase activity.

We have shown that vanadium mimics several insulin effects in rat adipocytes, via a staurosporine sensitive cytosolic protein tyrosine kinase (CytPTK; Shisheva, A., and Shechter, Y. (1993) J. Biol. Chem. 268, 6463). Here we demonstrate that vanadium effects on protein tyrosine kinases are preserved after cell disintegration. Vanadium inhibits or activates protein tyrosine kinases depending on its oxidation state and the tyrosine kinase studied. Vanadyl (4+) but not vanadate (5+) inhibits receptor tyrosine kinases such as the insulin receptor (IC50 value = 23 +/- 4 microM) and the insulin-like growth factor-I receptor (IC50 = 19 +/- 3 microM). Inhibition is non-competitive with respect to ATP, Mn2+, or substrate concentrations. Preincubation of adipocytes with vanadyl (0.4 mM), and staurosporine (which arrests the cytosolic enzyme) substantially inhibited insulin-stimulated lipogenesis. Vanadyl is readily oxidized to vanadate by hydrogen peroxide. In contrast, CytPTKs were poorly inhibited by vanadyl, and vanadate stimulated several CytPTKs 2-6 fold. CytPTK derived from rat adipocytes, liver and brain were activated, and CytPTK from Nb2 lymphoma cells was not affected. CytPTK extracted from insulin-responsive tissues are more sensitive to vanadate activation (ED50 = 3 +/- 0.7 microM), whereas the brain enzyme is less sensitive (ED50 = 27 +/- 3 microM). Tungstate, molybdate, and phenylarsine oxide also stimulate CytPTK, suggesting that the vanadate effect is secondary to inhibiting protein phosphotyrosine phosphatases. This study supports a working hypothesis implicating the intracellular vanadyl pool in modulating CytPTK activity. Any physiological conditions converting vanadyl to vanadate (i.e. H2O2 production) will activate CytPTK and consequently CytPTK-dependent bioeffects.

Adipocytes↗
PubMed2005

Oxidation of vanadium(III) by hydrogen peroxide and the oxomonoperoxo vanadium(V) ion in acidic aqueous solutions: a kinetics and simulation study.

The reaction between vanadium(III) and hydrogen peroxide in aqueous acidic solutions was investigated. The rate law shows first-order dependences on both vanadium(III) and hydrogen peroxide concentrations, with a rate constant, defined in terms of -d[H(2)O(2)]/dt, of 2.06 +/- 0.03 L mol(-)(1) s(-)(1) at 25 degrees C; the rate is independent of hydrogen ion concentration. The varying reaction stoichiometry, the appreciable evolution of dioxygen, the oxidation of 2-PrOH to acetone, and the inhibition of acetone formation by the hydroxyl radical scavengers, dimethyl sulfoxide and sodium benzoate, point to a Fenton mechanism as the predominant pathway in the reaction. Methyltrioxorhenium(VII) does not appear to catalyze this reaction. A second-order rate constant for the oxidation of V(3+) by OV(O(2))(+) was determined to be 11.3 +/- 0.3 L mol(-)(1) s(-)(1) at 25 degrees C. An overall reaction scheme consisting of over 20 reactions, in agreement with the experimental results and literature reports, was established by kinetic simulation studies.

Hydrogen Peroxide↗
PubMed2000

Selective determination method for vanadium (V) and vanadium (IV) controlling the pH of media for a solid-liquid extraction column.

Solid-liquid extraction separation based on a speciation method was studied for selective determination of vanadium (IV) and vanadium (V). Both V (IV) and V (V) cations transform to oxo-acid anion along with pH changes in the solution. The pH values for the transition points are different from each other and the difference was utilized in the separation. In the first step, particulate samples are dissolved by strong acids such as 1 M H2SO4 or 85% H3PO4. The pH of the strong acidic sample solutions of V (IV) and V (IV) are adjusted to the range between 3 and 4. In this condition, V (IV) is in the form of cation but V (V) is anion. The pH adjusted solution is applied to an anion exchange column. The solution is expected to contain V (IV) only. The trapped V (V) anion is eluted as VO2+ cation by a pH 1 acid. The author and coworker have already developed an HPLC separation method utilizing this separation concept. However, the HPLC method has some limitations, mainly originated in physical and chemical weaknesses of the HPLC column. In the present study, a firm solid-liquid column is adopted to replace the feeble HPLC column as a separation device. And a simple and convenient pH adjustment technique for making the sample solution is investigated at the same time. With these improvements, the speciation method developed with strong acidic solutions could determine the amount of V (IV) and V (V) in various environmental and biological samples.

Chromatography, High Pressure Liquid↗
PubMed2002

On-column complexation and simultaneous separation of vanadium(IV) and vanadium(V) by capillary electrophoresis with direct UV detection.

An on-column complexation method has been developed for the simultaneous determination of V(IV) and V(V). Vanadium species were chelated with aminopolycarboxylic acids to form anionic complexes which were separated by capillary zone electrophoresis (CZE) with direct UV detection. Ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentacetric acid (DTPA), nitrilotriacetic acid (NTA), and N-2-hydroxyethylethlendiaminetriacetric acid (HEDTA) were investigated as both ligand and running electrolyte. Of the ligands studied the complexes of EDTA with V(IV) and V(V) resulted in the highest selectivity and UV response. The conditions used for on-column complexation and separation, including pH, and electrolyte ligand concentration, were examined to achieve reasonable separation selectivity and detection sensitivity. The optimum separation of the anionic forms of V(IV) and V(V) was obtained by use of CZE with UV detection at 185 nm and an electrolyte containing 5 mmol L(-1) EDTA at pH 4.0. Linear calibration plots were obtained in the concentration range10-300 micro mol L(-1); detection limits were 3 micro mol L(-1) for V(IV) and 1 micro mol L(-1) for V(V). The proposed method was demonstrated for the determination of vanadium in groundwater spiked with V(IV) and V(V).

Edetic Acid↗
PubMed2001

Guanine versus deoxyribose damage in DNA oxidation mediated by vanadium(IV) and vanadium(V) complexes.

Vanadyl sulfate reacts with the peroxy acid oxidant KHSO5 to produce guanine-selective oxidation of a 167-bp restriction fragment of DNA. The oxidized lesions result in strand scission after hot piperidine treatment. Although several reactive intermediates are possible, quenching studies with ethanol and tert-butyl alcohol suggest that a monoperoxysulfate radical or a caged sulfate radical are the likely species responsible for oxidation of guanine. Several oxidants and various vanadium complexes (including insulin mimetic compounds) were studied with DNA for comparison. None of the other vanadium complexes showed modification of the double-stranded 167-bp fragment of DNA in the presence of KHSO5. The reactivity of VOSO4 may be due to its irreversible oxidation potential of 0.77 V (vs. Ag+/AgCl, pH 7.0, 10 mM phosphate), making it an appropriate catalyst for decomposition of monoperoxysulfate.

DNA Damage↗
PubMed1990

Characterization of vanadium bromoperoxidase from Macrocystis and Fucus: reactivity of vanadium bromoperoxidase toward acyl and alkyl peroxides and bromination of amines.

Vanadium bromoperoxidase (V-BrPO) has been isolated and purified from the marine brown algae Fucus distichus and Macrocystis pyrifera. V-BrPO catalyzes the oxidation of bromide by hydrogen peroxide, resulting in the bromination of certain organic acceptors or the formation of dioxygen. V-BrPO from F. distichus and M. pyrifera have subunit molecular weights of 65,000 and 74,000, respectively, and specific activities of 1580 units/mg (pH 6.5) and 1730 units/mg (pH 6) for the bromination of monochlorodimedone, respectively. As isolated, the enzymes contain a substoichiometric vanadium/subunit ratio; the vanadium content and specific activity are increased by addition of vanadate. V-BrPO (F. distichus, M. pyrifera, and Ascophyllum nodosum) also catalyzes the oxidation of bromide using peracetic acid. In the absence of an organic acceptor, a mixture of oxidized bromine species (e.g., hypobromous acid, bromine, and tribromide) is formed. Bromamine derivatives are formed from the corresponding amines, while 5-bromocytosine is formed from cytosine. In all cases, the rate of the V-BrPO-catalyzed reaction is much faster than that of the uncatalyzed oxidation of bromide by peracetic acid, at pH 8.5, 1 mM bromide, and 2 mM peracetic acid. In contrast to hydrogen peroxide, V-BrPO does not catalyze formation of dioxygen from peracetic acid in either the presence or absence of bromide. V-BrPO also uses phenylperacetic acid, m-chloroperoxybenzoic acid, and p-nitroperoxybenzoic acid to catalyze the oxidation of bromide; dioxygen is not formed with these peracids. V-BrPO does not catalyze bromide oxidation or dioxygen formation with the alkyl peroxides ethyl hydroperoxide, tert-butyl hydroperoxide, and cuminyl hydroperoxide.

Amines↗
PubMed2002

Modeling the catalytic site of vanadium bromoperoxidase: synthesis and structural characterization of intramolecularly H-bonded vanadium(V) oxoperoxo complexes, [VO(O(2))((NH)2pyg(2))]K and [VO(O(2))((BrNH)2pyg(2))]K.

Vanadium haloperoxidases (VHPO) catalyze the peroxidative halogenation of organic substrates. Crystallographic studies suggest that hydrogen bonding from a lysine side chain to the vanadium(V)-bound peroxo group may facilitate oxidation of halides (Cl(-), Br(-), I(-)). A ligand with pendant NH(2) functionality, N-(2-pyridylmethyl-6-amino) iminodiacetic acid (H(2)(NH)2pyg(2).2HCl) has been designed to explore the effects that H-bonding from Lys may have on peroxide activation. The first structural characterization of VBrPO model complexes [VO(O(2))((NH)2pyg(2))]K and [VO(O(2))((BrNH)2pyg(2))]K which demonstrate direct intramolecular H-bonding between an amine functionality and V(V)-bound peroxide is reported. The distances between NH(2) proton and bound peroxo moiety [(d(N(1)-H.O): 2.637(4) A in [VO(O(2))((NH)()2pyg(2))]K, and 2.640(8) and 2.6919(8) A in [VO(O(2))((BrNH)2pyg(2))]K] are indicative of intramolecular H-bonding. The intramolecular H-bond strength in [VO(O(2))((BrNH)2pyg(2))](-) is estimated at 6 kcal/mol by (1)H NMR studies and demonstrates that the H-bond interaction is also significant in solution.

Amines↗
PubMed1991

Tetravalent vanadium releases ferritin iron which stimulates vanadium-dependent lipid peroxidation.

The iron storage protein, ferritin, represents a possible source of iron for oxidative reactions in biological systems. It has been shown that superoxide and several xenobiotic free radicals can release iron from ferritin by a reductive mechanism. Tetravalent vanadium (vanadyl) reacts with oxygen to generate superoxide and pentavalent vanadium (vanadate). This led to the hypothesis that vanadyl causes the release of iron from ferritin. Therefore, the ability of vanadyl and vanadate to release iron from ferritin was investigated. Iron release was measured by monitoring the generation of the Fe(2+)-ferrozine complex. It was found that vanadyl but not vanadate was able to mobilize ferritin iron in a concentration dependent fashion. Initial rates, and iron release over 30 minutes, were unaffected by the addition of superoxide dismutase. Glutathione or vanadate added in relative excess to the concentration of vanadyl, inhibited iron release up to 45%. Addition of ferritin at the concentration used for measuring iron release prevented vanadyl-induced NADH oxidation. Vanadyl promoted lipid peroxidation in phospholipid liposomes. Addition of ferritin to the system stimulated lipid peroxidation up to 50% above that with vanadyl alone. Ferritin alone did not promote significant levels of lipid peroxidation.

Catalase↗
PubMed2004

N,N'-ethylenebis(pyridoxylideneiminato) and N,N'-ethylenebis(pyridoxylaminato): synthesis, characterization, potentiometric, spectroscopic, and DFT studies of their vanadium(IV) and vanadium(V) complexes.

The Schiff base N,N'-ethylenebis(pyridoxylideneiminato) (H(2)pyr(2)en, 1) was synthesized by reaction of pyridoxal with ethylenediamine; reduction of H(2)pyr(2)en with NaBH(4) yielded the reduced Schiff base N,N'-ethylenebis(pyridoxylaminato) (H(2)Rpyr(2)en, 2); their crystal structures were determined by X-ray diffraction. The totally protonated forms of 1 and 2 correspond to H(6)L(4+), and all protonation constants were determined by pH-potentiometric and (1)H NMR titrations. Several vanadium(IV) and vanadium(V) complexes of these and other related ligands were prepared and characterized in solution and in the solid state. The X-ray crystal structure of [V(V)O(2)(HRpyr(2)en)] shows the metal in a distorted octahedral geometry, with the ligand coordinated through the N-amine and O-phenolato moieties, with one of the pyridine-N atoms protonated. Crystals of [(V(V)O(2))(2)(pyren)(2)].2 H(2)O were obtained from solutions containing H(2)pyr(2)en and oxovanadium(IV), where Hpyren is the "half" Schiff base of pyridoxal and ethylenediamine. The complexation of V(IV)O(2+) and V(V)O(2) (+) with H(2)pyr(2)en, H(2)Rpyr(2)en and pyridoxamine in aqueous solution were studied by pH-potentiometry, UV/Vis absorption spectrophotometry, as well as by EPR spectroscopy for the V(IV)O systems and (1)H and (51)V NMR spectroscopy for the V(V)O(2) systems. Very significant differences in the metal-binding abilities of the ligands were found. Both 1 and 2 act as tetradentate ligands. H(2)Rpyr(2)en is stable to hydrolysis and several isomers form in solution, namely cis-trans type complexes with V(IV)O, and alpha-cis- and beta-cis-type complexes with V(V)O(2). The pyridinium-N atoms of the pyridoxal rings do not take part in the coordination but are involved in acid-base reactions that affect the number, type, and relative amount of the isomers of the V(IV)O-H(2)Rpyr(2)en and V(V)O(2)-H(2)Rpyr(2)en complexes present in solution. DFT calculations were carried out and support the formation and identification of the isomers detected by EPR or NMR spectroscopy, and the strong equatorial and axial binding of the O-phenolato in V(IV)O and V(V)O(2) complexes. Moreover, the DFT calculations done for the [V(IV)O(H(2)Rpyr(2)en)] system indicate that for almost all complexes the presence of a sixth equatorial or axial H(2)O ligand leads to much more stable compounds.

Journal Article↗
PubMed2005

New homoleptic organometallic derivatives of vanadium(III) and vanadium(IV): synthesis, characterization, and study of their electrochemical behaviour.

The arylation of [VCl3(thf)3] with LiR(Cl), where R(Cl) is a polychlorinated phenyl group [C6Cl5, 2,4,6-trichlorophenyl(tcp), or 2,6-dichlorophenyl (dcp)] gives four-coordinate, homoleptic organovanadium(III) derivatives with the formula [Li(thf)(4)][V(III)(R(Cl))(4)] (R(Cl) = C(6)Cl(5) (1), tcp (2), dcp (3)). The anion [V(III)(C6Cl5)4]- has an almost tetrahedral geometry, as observed in the solid-state structure of [NBu4][V(C6Cl5)4] (1') (X-ray diffraction). Compounds 1-3 are electrochemically related to the neutral organovanadium(IV) species [V(IV)(R(Cl))4] (R(Cl) = C6Cl5 (4), tcp (5), dcp (6)). The redox potentials of the V(IV)/V(III) semisystems in CH2Cl2 decrease with decreasing chlorination of the phenyl ring (E(1/2) = 0.84 (4/1), 0.42 (5/2), 0.25 V (6/3)). All the [V(IV)(R(Cl))4] derivatives involved in these redox couples could also be prepared and isolated by chemical methods. The arylation of [VCl(3)(thf)(3)] with LiC6F5 also gives a homoleptic organovanadium(III) compound, but with a different stoichiometry: [NBu4]2[V(III)(C6F5)5] (7). In this five-coordinate species, the C6F5 groups define a trigonal bipyramidal environment for the vanadium atom (X-ray diffraction). EPR spectra for the new organovanadium compounds 1-6 are also given and analysed in terms of an elongated tetrahedral structure with C(2v) local symmetry. It is suggested that the R(Cl) groups exert a protective effect towards the vanadium centre.

Journal Article↗