An extremely stable Ni(II) complex derived from the hydrolytic cleavage of the C-terminal tail of histone H2A

Marios Mylonas; John C Plakatouras; Nick Hadjiliadis; Konstantinos D Papavasileiou; Vasilios S Melissas

doi:10.1016/j.jinorgbio.2004.11.020

An extremely stable Ni(II) complex derived from the hydrolytic cleavage of the C-terminal tail of histone H2A

J Inorg Biochem. 2005 Feb;99(2):637-43. doi: 10.1016/j.jinorgbio.2004.11.020.

Authors

Marios Mylonas¹, John C Plakatouras, Nick Hadjiliadis, Konstantinos D Papavasileiou, Vasilios S Melissas

Affiliation

¹ Department of Chemistry, University of Ioannina, GR 451 10 Ioannina, Greece.

PMID: 15621298
DOI: 10.1016/j.jinorgbio.2004.11.020

Abstract

The C-terminal blocked tetrapeptides SHHK- and SAHK-, which represent the fragments produced from the hydrolysis of the hexapeptides' -TASHHK-, -TESHHK-, and -TESAHK- complexes with Ni(II), were synthesized and their interactions with Ni(II) ions were studied potentiometrically and spectroscopically. Both tetrapeptides interact strongly with Ni(II) ions leading to square-planar complexes with 4N {NH(2),2N(-),N(im)} coordination. The stability of the Ni-SHHK- complex is about 2 orders of magnitude higher than the Ni-SAHK- complex. Spectroscopic evidence and theoretical predictions suggest the positioning of the free imidazole ring, in the Ni-SHHK- complex, above the coordination plane, explaining the extra stability of the complex.

MeSH terms

Amino Acid Sequence
Drug Stability
Histones / chemical synthesis
Histones / chemistry*
Hydrolysis
In Vitro Techniques
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Structure
Nickel / chemistry*
Oligopeptides / chemical synthesis
Oligopeptides / chemistry
Peptide Fragments / chemical synthesis
Peptide Fragments / chemistry
Thermodynamics

Substances

Histones
Oligopeptides
Peptide Fragments
Nickel