Disease relevance of copper

• Alcaligenes xylosoxidans dissimilatory nitrite reductase: alanine substitution of the surface-exposed histidine 139l ligand of the type 1 copper center prevents electron transfer to the catalytic center [1].

High impact information on copper

• In contrast, for the (trimethylsilyl)methyl and vinyl groups, the selectivity depends on the kinetics of reductive elimination of the Cu(III) intermediate [2].
• Finally, oxidation of Cu(2+) to Cu(3+) has been studied by cyclic voltammetry in water, which revealed that the redox reaction occurs only when the copper cation is within the diamino-diimido compartment [3].
• In the solid state the Cu(III) complexes were mainly characterized by single-crystal X-ray diffraction analysis, whereas in solution their structural characterization was mainly based on (1)H NMR spectroscopy given the diamagnetic nature of the d(8) square-planar Cu(III) complexes [4].
• The results from both types of compounds indicate that the binding site is located in a pocket near the type 1 copper center [5].
• Direct STM investigation of cinchona alkaloid adsorption on Cu(III) [6].

Biological context of copper

• The focus of this work is on DNA damage by Cu(III) and oxysulfur radicals formed by the oxidation of S(IV) oxides by dissolved oxygen in the presence of Cu(II) tetraglycine complexes [7].
• Based on these results and the sequence alignments made against Zucchini ascorbate oxidase it is speculated that structural differences in the substrate-activation site (a 'blue', type 1 copper center) control the redox potential range as well as substrate specificity, and the cystine content contributes to stability [8].

Analytical, diagnostic and therapeutic context of copper

• A sequence analysis indicated that the P. cinnabarinus lcc3-1 product has a Phe residue at a position likely to influence the reduction-oxidation potential of the enzyme's type 1 copper center [9].

References