Sequence-Specific Cu(II)-Dependent Peptide Bond Hydrolysis: Similarities and Differences with the Ni(II)-Dependent Reaction
Author:
Affiliation:
1. Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ic5003176
Reference51 articles.
1. Interactions of Nickel(II) with Histones: Interactions of Nickel(II) with CH3CO-Thr-Glu-Ser-His-His-Lys-NH2, a Peptide Modeling the Potential Metal Binding Site in the “C-Tail” Region of Histone H2A
2. Ni(II) Specifically Cleaves the C-Terminal Tail of the Major Variant of Histone H2A and Forms an Oxidative Damage-Mediating Complex with the Cleaved-Off Octapeptide
3. The binding of Ni(ii) ions to terminally blocked hexapeptides derived from the metal binding -ESHH- motif of histone H2A
4. Sequence-specific Ni(II)-dependent peptide bond hydrolysis in a peptide containing threonine and histidine residues.
5. Sequence-Specific Ni(II)-Dependent Peptide Bond Hydrolysis for Protein Engineering. Combinatorial Library Determination of Optimal Sequences
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