Frączyk Tomasz
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Inorg Chem. 2021 Jun 21;60(12):8447-8450. doi: 10.1021/acs.inorgchem.1c00939. Epub 2021 Jun 7.
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.
氨基末端铜(II)和镍(II)结合(ATCUN)基序能强烈螯合铜(II)离子。然而,相邻残基磷酸化对这种络合作用的影响尚未阐明。使用光谱方法比较了来自人组蛋白-1和人血清白蛋白的原始肽和磷酸化肽的铜(II)解离常数。磷酸化显著减弱了铜(II)的结合。因此,这些结果表明磷酸化可能是控制金属离子结合的关键机制。