Alpha-benzilmonoxime has been used for the extraction and determination of cobalt at microgram amount. The reagent reacts with cobalt(II) in the pH range of 8.8 - 9.3 to form a yellow-color chelate, which is extracted in chloroform, toluene, and some other non-polar solvents. The chelate is stable in chloroform for about one day. Under the optimum conditions of the a-benzilmonoxime concentratio...

Several cobalt(II), copper(II) and nickel(II) complexes of nicotinoylhydrazine-derived compounds were prepared and characterised by physical, spectral and analytical data. These compounds and their complexes have proven to be antibacterial. The screening data show the metal complexes to be more potential/bactericidal than the uncomplexed compounds against one or more bacterial species.

To facilitate the study of individual metal binding sites of polymeric metalloproteins, conversion of exchange-labile Co(II) in E. coli alkaline phosphatase (EC 3.1.3.1) to exchange-inert Co(III) was examined. Oxidation of Co(II) alkaline phosphatase with hydrogen peroxide results in a single absorption maximum at 530 nm and loss both of the characteristic electron paramagnetic signal and of en...

Pentafluorophenylboron-capped iron and cobalt(II) hexachloroclathrochelate precursors were obtained by the one-pot template condensation of dichloroglyoxime with pentafluorophenylboronic acid on iron and cobalt(II) ions under vigorous reaction conditions in trifluoroacetic acid media. These reactive precursors easily undergo nucleophilic substitution with (per)fluoroarylthiolate anions, giving ...

http://sro.sussex.ac.uk Loukopoulos, Edward, Berkoff, Benjamin, Griffiths, Kieran, Keeble, Victoria, Dokorou, Vassiliki N, Tsipis, Athanassios C, Escuer, Albert and Kostakis, George E (2015) Cobalt(II/III), nickel(II) and copper(II) coordination clusters employing a monoanionic Schiff base ligand: synthetic, topological and computational mechanistic aspects. CrystEngComm, 17 (35). pp. 6753-6764...

A cobalamin (Cbl) cofactor in corrinoid iron-sulfur protein (CoFeSP) is the primary methyl group donor and acceptor in biological carbon oxide conversion along the reductive acetyl-CoA pathway. Changes of the axial coordination of the cobalt ion within the corrin macrocycle upon redox transitions in aqua-, methyl-, and cyano-Cbl bound to CoFeSP or in solution were studied using X-ray absorption...