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2006 | 53 | 4 | 721-727
Article title

Sequence-specific Ni(II)-dependent peptide bond hydrolysis in a peptide containing threonine and histidine residues

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EN
Abstracts
EN
Previously we demonstrated that Ni(II) complexes of Ac-Thr-Glu-Ser-His-His-Lys-NH2 hexapeptide, representing residues 120-125 of human histone H2A, and some of its analogs undergo E-S peptide bond hydrolysis. In this work we demonstrate a similar coordination and reactivity pattern in Ni(II) complexes of Ac-Thr-Glu-Thr-His-His-Lys-NH2, its threonine analogue, studied using potentiometry, electronic absorption spectroscopy and HPLC. For the first time we present the detailed temperature and pH dependence of such Ni(II)-dependent hydrolysis reactions. The temperature dependence of the rate of hydrolysis yielded activation energy Ea = 92.0 kJ mol-1 and activation entropy ΔS≠ = 208 J mol-1 K-1. The pH profile of the reaction rate coincided with the formation of the four-nitrogen square-planar Ni(II) complex of Ac-Thr-Glu-Thr-His-His-Lys-NH2. These results expand the range of protein sequences susceptible to Ni(II) dependent cleavage by those containing threonine residues and permit predictions of the course of this reaction at various temperatures and pH values.
Publisher

Year
Volume
53
Issue
4
Pages
721-727
Physical description
Dates
published
2006
received
2006-07-19
revised
2006-10-31
accepted
2006-11-02
(unknown)
2006-11-22
Contributors
  • Department of Preventive Medicine and Community Health, University of Texas Medical Branch, Galveston, USA
  • University of Ioannina, Department of Chemistry, Ioannina, Greece
author
  • Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland
author
  • Central Institute of Labour Protection-National Research Institute, Warszawa, Poland
References
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv53p721kz
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