Ni (ii) ions are able to hydrolyze Naa-(Ser/Thr) peptide bonds in Naa-(Ser/Thr)-Xaa-His-Zaa
sequences. We found that various human transcription factors contain such nickel hydrolytic …

In this work we demonstrate that the previously described reaction of sequence specific Ni
(ii)-dependent hydrolytic peptide bond cleavage can be performed in complex …

Cu (I) exhibits high affinity for thiolate ligands, suggesting that thiol-rich zinc or iron binding
sites may be subject to disruption during copper stress conditions. Zinc fingers constitute a …

The elucidation of mechanisms by which cysteine (Cys) redox reactions influence metal
binding to zinc finger domains is important for understanding the structure and function of …

Zinc finger structures are frequently found in transcription factors and DNA repair proteins,
mediating DNA-protein and protein-protein binding. As low concentrations of transition metal …

Toxic and/or carcinogenic consequences may result from metal ionsubstitution for the Zn-(II)
in transcription factors containing zinc fingers, and the small Cys-rich metal-binding protein …

Nickel has been shown to be an essential trace element involved in the metabolism of
several species of bacteria, archea, and plants. In these organisms, nickel is involved in …

Zinc fingers (ZFs) are among the most abundant motifs found in proteins, and are commonly
known for their structural role. Classical ZFs (CCHH) are part of the transcription factors that …

A combined pH-metric and spectroscopic (UV/vis, CD, NMR) study of the Ni (II) binding to
CH3CO-Thr-Glu-Ser-His-His-Lys-NH2 (AcTESHHKam), a blocked hexapeptide modeling a …

Lead (Pb), mercury (Hg), and cadmium (Cd) are toxic and interfere with protein metal-
binding sites. The Cys2/His2 zinc finger is a structural motif required for sequence-specific …