Molecular and supramolecular features of oxo-peroxovanadium complexes containing O3N, O2N2and ON3donor sets

Časný, Marian; Rehder, Dieter

doi:10.1039/b315291j

Cited by 43 publications

(5 citation statements)

References 41 publications

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“…20 The binding constants reported for the vanadate-transferrin complex are pK 1 51 V values between 570 and 625 ppm are typical for oxo-monoperoxovanadium complexes with three-and four-dentate ON-ligands. 25 The resonance at 594 ppm observed in the vanadate-transferrin-H 2 O 2 system, clearly distinct from those of free peroxovanadate at pH 7.6 (Table 1), can therefore unambiguously be ascribed to a VO O 2 C -Tf complex. Addition of vanadate to acid phosphatase yields a strong signal at 541 ppm (including a shoulder at 539 ppm) along with two minor component at 487 and 515 ppm.…”

Section: Resultsmentioning

confidence: 90%

A vanadium‐51 NMR study of the binding of vanadate and peroxovanadate to proteins

Rehder

Časný

Große

2004

Magnetic Reson in Chemistry

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51V quadrupolar central transition NMR spectra of buffered (pH 7.6-8.0) solutions of bovine apo-transferrin (Tf) and bovine prostatic acid phosphatase (Pp) treated with vanadate show normal features (chemical shifts between -515 and -542 ppm) corresponding to the complexation of VO2+ to the Tf binding site and the Pp active centre, respectively. Addition of H2O2 leads to the temporary formation of complexed VO(O2)+ (delta approximately -595). Vanadate-dependent bromoperoxidase from the alga Ascophyllum nodosum exhibits an unusually high shielding both for the native (delta = -931) and the peroxo form (delta = -1135) of the enzyme. A resonance at -471 ppm is traced back to an inactive form with oxovanadium(V) in a trigonal-bipyramidal array.

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Section: Resultsmentioning

confidence: 90%

A vanadium‐51 NMR study of the binding of vanadate and peroxovanadate to proteins

Rehder

Časný

Große

2004

Magnetic Reson in Chemistry

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“…24 In addition, the complex exhibits an intense ν(V = O) stretch at 965 cm −1 . 25 The formation of the peroxido complex 7 has also been established in solution by the treatment of 4 with H 2 O 2 and following the changes by electronic absorption spectroscopy. Thus, drop-wise addition of aqueous 30% H 2 O 2 dissolved in methanol to 10 mL of a ca.…”

Section: Structural Models Of Haloperoxidasesmentioning

confidence: 99%

“…Spin Hamiltonian parameters obtained for [V IV O(acac)(sal-aepy)] (17) and PS-[V IV O(acac)(sal-aepy)](25) 29. …”

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confidence: 99%

Structural models of vanadate-dependent haloperoxidases, their reactivity, immobilization on polymer support and catalytic activities

Maurya

2011

J Chem Sci

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The design of structural and functional models of enzymes vanadate-dependent haloperoxidases (VHPO) and the isolation and/or generation of species having {VO(H 2 O)}, {VO 2 }, {VO(OH)} and {VO(O 2 )} cores, proposed as intermediate(s) during catalytic action, in solution have been studied. Catalytic potential of these complexes have been tested for oxo-transfer as well as oxidative bromination and sulfide oxidation reactions. Some of the oxidovanadium(IV) and dioxidovanadium(V) complexes have been immobilized on polymer support in order to improve their recycle ability during catalytic activities and turn over number. The formulations of the polymer-anchored complexes are based on the respective neat complexes and conclusions drawn from the various characterization studies. These catalysts have successfully been used for all catalytic reactions mentioned above. These catalysts are stable and recyclable.

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“…The most prominent application of VO x based catalysts probably is the production of sulphuric acid from SO 2 , an issue which also bears environmental aspects, namely atmospheric conversion of SO 2 to H 2 SO 4 . The antibiofouling properties of V 2 O 5 nano-wires, 10 65 In the case of {LVO}, an intermittently formed {LVO(OOH)} is the most likely target for the nucleophilic attack, at the hydroperoxido group, by a substrate such as SRR′. 66 A {VO(OOH)} intermediate is definitely not the active species, as heterogeneous catalysts such as 'vanadia' (V 2 O 5 ) are employed in oxidation reactions.…”

Section: The Potentiality Of Vanadates and Vanadium Oxidesmentioning

confidence: 99%

The future of/for vanadium

2013

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Vanadium compounds are stored or employed by several groups of bacterial and eukaryotic organisms. Two types of vanadium-dependent enzymes have so far been characterised: vanadate-dependent haloperoxidases from fungi, lichens, marine macroalgae and Streptomyces bacteria, and vanadium nitrogenases in proteo- and cyanobacteria. Several bacterial strains can employ vanadate(V) as an external electron acceptor in respiration, reducing vanadate to VO(2+) and thus contributing to the mineralisation of vanadium and to the detoxification of vanadate-contaminated water. Amanita mushrooms and many sea squirts accumulate vanadium, without the importance of this practise being well understood. Further, the analogy between vanadate and phosphate implicates an interference of vanadate with metabolic processes involving phosphate, suggesting a regulatory role for vanadate in most if not all organisms, including humans, but also hinting at toxic effects at unphysiologically high vanadate concentrations. The antidiabetic effect of vanadium compounds is probably related to the phosphate-vanadate antagonism, as is the potentiality of vanadate in the amelioration of cardiovascular affliction. The anti-cancer action of vanadium compounds and their in vitro activity towards the protozoa causing amoebiasis, leishmaniasis and Chagas' disease again may be rooted in the intervention of vanadate with the activity of phosphatases and kinases. In addition, most likely the ability of vanadate(V) and oxidovanadium(IV) to regulate the cellular production of reactive oxygen species comes in, thus influencing cellular signalling. Future developments of vanadium chemistry are likely to emphasize topics related to biological, environmental and medicinal aspects. Condensation of monovanadate results in the formation of oligovanadates, polyvanadates and finally colloidal and solid vanadium oxides that, in part, convey bio-mimetic functions comparable to those of simple vanadate, including its catalytic potential as an active centre in haloperoxidases and the lethal action against viruses, bacteria and protozoan parasites. Decavanadate has been shown to be stabilised by docking to proteins, and by integration into nanoscopic water pools of intracellular compartments, modelled by reverse micelles. The well established and approved use of vanadium oxides in, amongst other applications, catalysis has been recently impacted by the elucidation of the active surface species--VO(x)--of catalysts based on mixed vanadium oxides, and vanadium oxides on supports. Finally, materials based on vanadium oxides and vanadates play an increasingly important role as cathode materials in high density lithium batteries. An example is Ag2VO2PO4, which, in the discharge process, is reduced to Li(3.2)VO2PO4 and Ag. Oncoming developments in vanadium chemistry thus include oxide-based materials.

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Molecular and supramolecular features of oxo-peroxovanadium complexes containing O₃N, O₂N₂and ON₃donor sets

Cited by 43 publications

References 41 publications

A vanadium‐51 NMR study of the binding of vanadate and peroxovanadate to proteins

A vanadium‐51 NMR study of the binding of vanadate and peroxovanadate to proteins

Structural models of vanadate-dependent haloperoxidases, their reactivity, immobilization on polymer support and catalytic activities

The future of/for vanadium

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