In the crystal structure of the title compound, [CuCl(C(5)H(5)N)(4)][N(CN)(2)]·2C(6)H(5)N, the copper(II) cations are coordinated by one chloride anion and four N-bonded pyridine ligands into discrete complexes. The copper(II) cation shows a square-pyramidal coordination environment, with the chloride anion in the apical position. However, there is one additional chloride anion at 3.0065 (9) Å,...

The growth-promoting effect of the addition of 0-1 yo copper sulphate (supplying 250 p.p.m. Cu) to a growing-pig diet, reported by Barber, Braude, Mitchell & Cassidy (1955), has since been confirmed in many experiments both in Europe and America. In the present paper results of four further experiments are given dealing with: ( I ) the optimal level of copper sulphate to include in the diet; (2...

An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral...

The rate constants of the reactions between pulse radiolytically produced superoxide radicals and the Cu(II) chelate of diethyldithiocarbamate were determined at pH 7.0. It was found that diethyldithiocarbamate forms a copper complex, which as no dismutating activity. The removal of the protein bound copper in superoxide dismutase by diethyldithiocarbamate yields the same effect as coordination...

Copper enhances amyloid cytotoxicity and mediates human islet amyloid polypeptide (hIAPP) oligomerization; nickel, a redox inactive metal with similar protein binding affinity to copper, also mimics this effect, thereby demonstrating copper-mediated hIAPP cytotoxicity is due mainly to granular oligomer generation rather than ROS accumulation in type 2 diabetes.

The central importance of solvent interactions in stabilization of specific protein structure has long been recognized. Decades ago, Tanford and Kirkwood treated in detail the interaction of charges with solvent, and they showed how desolvation/burial of charges upon protein folding was an important factor in stability.1 The influence of their model, with further elaborations, can still be seen...

A novel copper-depleted bovine serum amine oxidase (BSAO), in which about half the molecules contained the organic cofactor in the oxidized form, was prepared by adding a reductant in anaerobic conditions to the cyanide-reacted protein. The CuI-semiquinone formed in these conditions reoxidizes after the removal of copper. The inactive derivative was reduced by benzylamine at approx. 1/1000 the ...

Copper (II) phthalocyanine and 2, 9, 16, 23 tetrakis nitro copper (II) phthalocyanine has been synthesized respectively from phthalonitrile and 4-nitro phthalonitrile under solvent-free condition using two different catalysts over nanodimensional zeolites. 4-Nitro phthalonitrile synthesized from phthaimide in three steps. The newly prepared compounds have been characterized by IR, UV-Vis,1H N...

Type zero copper is a hard-ligand analogue of the classical type 1 or blue site in copper proteins that function as electron transfer (ET) agents in photosynthesis and other biological processes. The EPR spectroscopic features of type zero Cu(II) are very similar to those of blue copper, although lacking the deep blue color, due to the absence of thiolate ligation. We have measured the rates of...

A systematic theoretical study on reaction mechanisms for copper(I)-catalyzed C-O coupling of phenols with aryl bromides is reported herein. Through evaluation of the relative concentrations of possible copper species in reaction solution and reactivity study of these copper species with aryl halides in the context of several commonly proposed mechanisms for copper(I)-catalyzed Ullmann reaction...