Copper(II), nickel(II) and zinc(II) complexes of N-acetyl-His-Pro-His-His-NH2

Equilibria, solution structure and enzyme mimicking

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The copper(II), nickel(II) and zinc(II) binding ability of the multi-histidine peptide N-acetyl-His-Pro-His-His-NH2 has been studied by combined pH-potentiometry and visible, CD and EPR spectroscopies. The internal proline residue, preventing the metal ion induced successive amide deprotonations, resulted in the shift of this process toward higher pH values as compared to other peptides. The metal ions in the parent [ML]2+ complexes are exclusively bound by the three imidazole side chains. In [CuH-1L]+, formed between pH 6-8, the side chains of the two adjacent histidines and the peptide nitrogen between them are involved in metal ion binding. The next deprotonation results in the proton loss of the coordinated water molecule (CuH-1L(OH)). The latter two species exert polyfunctional catalytic activity, since they possess superoxide dismutase-, catecholase- (the oxidation of 3,5-di-tert-butylcatechol) and phosphatase-like (transesterification of the activated phosphoester 2-hydroxypropyl-4-nitrophenyl phosphate) properties. On further increase of the pH rearrangement of the coordination sphere takes place leading to the [CuH-3L]- species, the deprotonated amide nitrogen displaces a coordinated imidazole nitrogen from the equatorial position of the metal ion. The shapes of the visible and CD spectra reflect a distorted arrangement of the donor atoms around the metal ion. In presence of zinc(II) the species [ZnL]2+ forms only above pH 6, which is shortly followed by precipitation. On the other hand, the [NiL]2+ complex is stable over a wide pH range, its deprotonation takes place only above pH 8. At pH 10 an octahedral NiH-2L species is present at first, which transforms slowly to a yellow square planar complex.

Original languageEnglish
Pages (from-to)1438-1448
Number of pages11
JournalJournal of Inorganic Biochemistry
Volume102
Issue number7
DOIs
Publication statusPublished - Jul 2008

Fingerprint

Nickel
Metal ions
Zinc
Copper
Deprotonation
Enzymes
Nitrogen
Metals
Ions
Histidine
Amides
Peptides
Transesterification
Phosphoric Monoester Hydrolases
Proline
Potentiometry
Superoxide Dismutase
Paramagnetic resonance
Protons
Catalyst activity

Keywords

  • Catecholase activity
  • Equilibrium studies
  • Histidine-rich peptides
  • Peptide complexes
  • SOD activity

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

@article{10aa963b3a424d2383aff76f1b7b5dec,
title = "Copper(II), nickel(II) and zinc(II) complexes of N-acetyl-His-Pro-His-His-NH2: Equilibria, solution structure and enzyme mimicking",
abstract = "The copper(II), nickel(II) and zinc(II) binding ability of the multi-histidine peptide N-acetyl-His-Pro-His-His-NH2 has been studied by combined pH-potentiometry and visible, CD and EPR spectroscopies. The internal proline residue, preventing the metal ion induced successive amide deprotonations, resulted in the shift of this process toward higher pH values as compared to other peptides. The metal ions in the parent [ML]2+ complexes are exclusively bound by the three imidazole side chains. In [CuH-1L]+, formed between pH 6-8, the side chains of the two adjacent histidines and the peptide nitrogen between them are involved in metal ion binding. The next deprotonation results in the proton loss of the coordinated water molecule (CuH-1L(OH)). The latter two species exert polyfunctional catalytic activity, since they possess superoxide dismutase-, catecholase- (the oxidation of 3,5-di-tert-butylcatechol) and phosphatase-like (transesterification of the activated phosphoester 2-hydroxypropyl-4-nitrophenyl phosphate) properties. On further increase of the pH rearrangement of the coordination sphere takes place leading to the [CuH-3L]- species, the deprotonated amide nitrogen displaces a coordinated imidazole nitrogen from the equatorial position of the metal ion. The shapes of the visible and CD spectra reflect a distorted arrangement of the donor atoms around the metal ion. In presence of zinc(II) the species [ZnL]2+ forms only above pH 6, which is shortly followed by precipitation. On the other hand, the [NiL]2+ complex is stable over a wide pH range, its deprotonation takes place only above pH 8. At pH 10 an octahedral NiH-2L species is present at first, which transforms slowly to a yellow square planar complex.",
keywords = "Catecholase activity, Equilibrium studies, Histidine-rich peptides, Peptide complexes, SOD activity",
author = "Jakab, {No{\'e}mi I.} and A. Jancs{\'o} and T. Gajda and B. Gyurcsik and A. Rockenbauer",
year = "2008",
month = "7",
doi = "10.1016/j.jinorgbio.2008.01.006",
language = "English",
volume = "102",
pages = "1438--1448",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Inc.",
number = "7",

}

TY - JOUR

T1 - Copper(II), nickel(II) and zinc(II) complexes of N-acetyl-His-Pro-His-His-NH2

T2 - Equilibria, solution structure and enzyme mimicking

AU - Jakab, Noémi I.

AU - Jancsó, A.

AU - Gajda, T.

AU - Gyurcsik, B.

AU - Rockenbauer, A.

PY - 2008/7

Y1 - 2008/7

N2 - The copper(II), nickel(II) and zinc(II) binding ability of the multi-histidine peptide N-acetyl-His-Pro-His-His-NH2 has been studied by combined pH-potentiometry and visible, CD and EPR spectroscopies. The internal proline residue, preventing the metal ion induced successive amide deprotonations, resulted in the shift of this process toward higher pH values as compared to other peptides. The metal ions in the parent [ML]2+ complexes are exclusively bound by the three imidazole side chains. In [CuH-1L]+, formed between pH 6-8, the side chains of the two adjacent histidines and the peptide nitrogen between them are involved in metal ion binding. The next deprotonation results in the proton loss of the coordinated water molecule (CuH-1L(OH)). The latter two species exert polyfunctional catalytic activity, since they possess superoxide dismutase-, catecholase- (the oxidation of 3,5-di-tert-butylcatechol) and phosphatase-like (transesterification of the activated phosphoester 2-hydroxypropyl-4-nitrophenyl phosphate) properties. On further increase of the pH rearrangement of the coordination sphere takes place leading to the [CuH-3L]- species, the deprotonated amide nitrogen displaces a coordinated imidazole nitrogen from the equatorial position of the metal ion. The shapes of the visible and CD spectra reflect a distorted arrangement of the donor atoms around the metal ion. In presence of zinc(II) the species [ZnL]2+ forms only above pH 6, which is shortly followed by precipitation. On the other hand, the [NiL]2+ complex is stable over a wide pH range, its deprotonation takes place only above pH 8. At pH 10 an octahedral NiH-2L species is present at first, which transforms slowly to a yellow square planar complex.

AB - The copper(II), nickel(II) and zinc(II) binding ability of the multi-histidine peptide N-acetyl-His-Pro-His-His-NH2 has been studied by combined pH-potentiometry and visible, CD and EPR spectroscopies. The internal proline residue, preventing the metal ion induced successive amide deprotonations, resulted in the shift of this process toward higher pH values as compared to other peptides. The metal ions in the parent [ML]2+ complexes are exclusively bound by the three imidazole side chains. In [CuH-1L]+, formed between pH 6-8, the side chains of the two adjacent histidines and the peptide nitrogen between them are involved in metal ion binding. The next deprotonation results in the proton loss of the coordinated water molecule (CuH-1L(OH)). The latter two species exert polyfunctional catalytic activity, since they possess superoxide dismutase-, catecholase- (the oxidation of 3,5-di-tert-butylcatechol) and phosphatase-like (transesterification of the activated phosphoester 2-hydroxypropyl-4-nitrophenyl phosphate) properties. On further increase of the pH rearrangement of the coordination sphere takes place leading to the [CuH-3L]- species, the deprotonated amide nitrogen displaces a coordinated imidazole nitrogen from the equatorial position of the metal ion. The shapes of the visible and CD spectra reflect a distorted arrangement of the donor atoms around the metal ion. In presence of zinc(II) the species [ZnL]2+ forms only above pH 6, which is shortly followed by precipitation. On the other hand, the [NiL]2+ complex is stable over a wide pH range, its deprotonation takes place only above pH 8. At pH 10 an octahedral NiH-2L species is present at first, which transforms slowly to a yellow square planar complex.

KW - Catecholase activity

KW - Equilibrium studies

KW - Histidine-rich peptides

KW - Peptide complexes

KW - SOD activity

UR - http://www.scopus.com/inward/record.url?scp=44649085703&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=44649085703&partnerID=8YFLogxK

U2 - 10.1016/j.jinorgbio.2008.01.006

DO - 10.1016/j.jinorgbio.2008.01.006

M3 - Article

VL - 102

SP - 1438

EP - 1448

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 7

ER -