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

• Authors: Artur Krężel , Marios Mylonas , Edyta Kopera , Wojciech Bal
• Languages of publication: 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.

Keywords

EN

activation parameters; complex formation; nickel(II); peptide bond hydrolysis

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2006
• Volume: 53
• Issue: 4
• Pages: 721-727

Dates

published

2006

received

2006-07-19

revised

2006-10-31

accepted

2006-11-02

(unknown)

2006-11-22

Contributors

author

Artur Krężel

• Department of Preventive Medicine and Community Health, University of Texas Medical Branch, Galveston, USA

author

Marios Mylonas

• University of Ioannina, Department of Chemistry, Ioannina, Greece

author

Edyta Kopera

• Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland

author

Wojciech Bal

• Central Institute of Labour Protection-National Research Institute, Warszawa, Poland

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