Outputs (2)

CopC Protein from Pseudomonas fluorescens SBW25 Features a Conserved Novel High-Affinity Cu(II) Binding Site (2015)
Journal Article
Wijekoon, C. J., Young, T. R., Wedd, A. G., & Xiao, Z. (2015). CopC Protein from Pseudomonas fluorescens SBW25 Features a Conserved Novel High-Affinity Cu(II) Binding Site. Inorganic Chemistry, 54(6), 2950-2959. https://doi.org/10.1021/acs.inorgchem.5b00031

Copper homeostasis in the bacterium Pseudomonas fluorescens SBW25 appears to be mediated mainly via chromosomal cue and cop systems. Under elevated copper levels that induce stress, the cue system is activated for expression of a P1B-type ATPase to r... Read More about CopC Protein from Pseudomonas fluorescens SBW25 Features a Conserved Novel High-Affinity Cu(II) Binding Site.

A set of robust fluorescent peptide probes for quantification of Cu(II) binding affinities in the micromolar to femtomolar range (2015)
Journal Article
Young, T. R., Wijekoon, C. J., Spyrou, B., Donnelly, P. S., Wedd, A. G., & Xiao, Z. (2015). A set of robust fluorescent peptide probes for quantification of Cu(II) binding affinities in the micromolar to femtomolar range. Metallomics, 7(3), 567-578. https://doi.org/10.1039/c4mt00301b

Reliable quantification of copper binding affinities and identification of the binding sites provide a molecular basis for an understanding of the nutritional roles and toxic effects of copper ions. Sets of chromophoric probes are now available that... Read More about A set of robust fluorescent peptide probes for quantification of Cu(II) binding affinities in the micromolar to femtomolar range.