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Phosphorylation impacts Cu(II) binding by ATCUN motifs

Frączyk, Tomasz (2021) Phosphorylation impacts Cu(II) binding by ATCUN motifs. Inorganic Chemistry . ISSN Print Edition ISSN: 0020-1669 Web Edition ISSN: 1520-510X

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Official URL: https://pubs.acs.org/doi/10.1021/acs.inorgchem.1c0...


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.

Item Type:Article
Subjects:Q Science > Q Science (General)
Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions:Department of Biophysics
ID Code:2042
Deposited By: Tomasz Frączyk
Deposited On:14 Jun 2021 14:48
Last Modified:14 Jun 2021 14:48

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