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Phosphorylation impacts Cu(II) binding by ATCUN motifs

Object's details: Phosphorylation impacts Cu(II) binding by ATCUN motifs

tile.noImage

Provider:Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

Description

Title:
Phosphorylation impacts Cu(II) binding by ATCUN motifs
Creator:
Frączyk, Tomasz
Description:
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.
Object availability:
free access
Date:
2021
Type:
Article;
PeerReviewed
Language:
English;
eng
Format:
application/pdf
Publisher:
ACS Publications
Relation: http://eprints.ibb.waw.pl/2042 ;https://pubs.acs.org/doi/10.1021/acs.inorgchem.1c00939 ;
10.1021/acs.inorgchem.1c00939
Subject:
Q Science (General);
QD Chemistry;
QH301 Biology
Identifier: http://eprints.ibb.waw.pl/2042/1/acs.inorgchem.1c00939.pdf ;
Frączyk, Tomasz (2021) Phosphorylation impacts Cu(II) binding by ATCUN motifs. Inorganic Chemistry . ISSN Print Edition ISSN: 0020-1669 Web Edition ISSN: 1520-510X
Data provider:
Repozytorium Instytutu Biochemii i Biofizyki Polskiej Akademii Nauk

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