The copper chaperone for superoxide dismutase (CCS) activates the antioxidant enzyme Cu, Zn SOD (SOD1) by directly inserting the copper cofactor into the apo form of SOD1. Neither the mechanism of protein-protein recognition nor of metal transfer is clear. The metal transfer step has been proposed to occur within a transient copper donor/ acceptor complex that is either a heterodimer or heterot...

The copper chaperone for superoxide dismutase (CCS) activates the antioxidant enzyme Cu,Zn-SOD (SOD1) by directly inserting the copper cofactor into the apo form of SOD1. Neither the mechanism of protein-protein recognition nor of metal transfer is clear. The metal transfer step has been proposed to occur within a transient copper donor/acceptor complex that is either a heterodimer or heterotet...

Cytotoxic activities of acetoacetanilide N(4)-methyl(phenyl)thiosemicarbazone (L2H) and its seven different metal complexes were studied. Of these, IC50 value of the copper complex was found to be 46 μg/ml. Antitumour studies of this copper complex was carried out using Daltons Lymphoma Ascites cell-induced solid tumour model and Ehrlich's Ascites Carcinoma cell-induced ascites tumour model. Ad...

The titration of methanobactin with Cu(II) was monitored by both UV/Vis and NMR spectroscopy and indicates that the major transitions occurring when Cu(II) interacts with methanobactin involve a two-step process that is complete by about 0.6 Cu:mb. This suggests that a 2:1 complex is formed between methanobactin and copper at low copper levels. If this complex exists, it would be different than...