Several mammalian enzymes catalyzing the phosphorolytic-arsenolytic cleavage of their substrates (thus yielding arsenylated metabolites) have been shown to facilitate reduction of arsenate (AsV) to the more toxic arsenite (AsIII) in presence of their substrate and a thiol. These include purine nucleoside phosphorylase (PNP), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and glycogen phospho...

The highly explosive molecules As(N(3))(3) and Sb(N(3))(3) were obtained in pure form by the reactions of the corresponding fluorides with (CH(3))(3)SiN(3) in SO(2) and purification by sublimation. The crystal structures and (14)N NMR, infrared, and Raman spectra were determined, and the results compared to ab initio second-order perturbation theory calculations. Whereas Sb(N(3))(3) possesses a...

Arsenic (atomic number, 33; relative atomic mass, 74.92) has chemical and physical properties intermediate between a metal and a nonmetal, and is often referred to as a metalloid or semi-metal. It belongs to Group VA of the Periodic Table, and can exist in four oxidation states: –3, 0, +3, and +5. Arsenite, AsIII, and arsenate, AsV, are the predominant oxidation states under, respectively, redu...

Lacunary polyoxometalates (POMs) are negatively charged metal–oxo clusters, formally obtained from plenary topologies via fragment removal. Owing to the removal, lacunary POMs archetypes rich in nucleophilic terminal oxo ligands, making them suitable for post-synthetic coordination with various heterometals. Trilacunary heteropolytungstates (hetero-POTs) based on bowl-shaped {W9O30} framework i...

The environmentally prevalent arsenate (AsV) is reduced in the body to the much more toxic arsenite (AsIII). Recently, we have demonstrated that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the reduction of AsV in the presence of glutathione, yet the role of GAPDH in AsV reduction in vivo is unknown. Therefore, we examined the effect of (S)-alpha-cholorhydrin...

The mammalian enzymes responsible for reduction of the environmentally prevalent arsenate (AsV) to the much more toxic arsenite (AsIII) are unknown. In the previous paper (Nemeti and Gregus, 2005), we proposed that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and/or phosphoglycerate kinase (PGK) may catalyze reduction of AsV in human red blood cells (RBC), hemolysate, or rat liver cytosol. ...