Phosphorylation Impacts Cu(II) Binding by ATCUN Motifs

ATCUN (amino terminal Cu(II) and Ni(II) binding) motifs chelate Cu(II) ions strongly. However, the impact of the phosphorylation of neighboring residues on such complexation has not been elucidated. The copper(II) dissociation constants of original and phosphorylated peptides from human histatin-1 and human serum albumin were compared using spectroscopic methods. Phosphorylation markedly weakened Cu(II) binding. Thus, these results indicate that phosphorylation may be a vital mechanism governing metal ion binding.

Automated summary

The study compared the effect of phosphorylation on copper(II) binding in peptides from human histatin-1 and human serum albumin, revealing that phosphorylation markedly weakened the binding of Cu(II). This suggests that phosphorylation may play a vital role in regulating metal ion binding.