Copper and zinc binding properties of the N-terminal histidine-rich sequence of Haemophilus ducreyi Cu,Zn superoxide dismutase

Paksi, Z.; Jancsó, Attila; Pacello, Francesca; Nagy, Nóra Veronika; Battistoni, Andrea; Gajda, Tamás

doi:10.1016/j.jinorgbio.2008.04.007

Cited by 36 publications

(36 citation statements)

References 44 publications

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“…In proteins and peptides, mercury(II) is known to have an outstanding affinity for the soft sulfur ligands and a strong preference for linear [56][57][58][59] or trigonal coordination geometries [59][60][61][62], however, it can also adopt a tetrahedral coordination environment of donor groups [63][64][65]. In contrast, cadmium(II) and zinc(II) prefer tetrahedral coordination geometry [55,59,65], but higher 15 coordination numbers are also easily possible, especially for the more flexible zinc(II) ions [55,66]. The binding affinities of d 10 metal ions to cysteine follow the order of Hg 2+ > Cd 2+ > Zn 2+ [67,68] which usually also stands for metallothioneins [67] and MerR metalloregulatory proteins [68].…”

Section: Competition Of Zinc(ii) With Cadmium(ii) or Mercury(ii) In Bmentioning

confidence: 99%

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Jancsó

Gyurcsik

Mesterházy

et al. 2013

Journal of Inorganic Biochemistry

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Section: Competition Of Zinc(ii) With Cadmium(ii) or Mercury(ii) In Bmentioning

confidence: 99%

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Jancsó

Gyurcsik

Mesterházy

et al. 2013

Journal of Inorganic Biochemistry

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“…At twofold metal ion excess dinuclear complexes are formed, similarly to other multihistidine peptides [12,39]. The UV-Vis, CD and EPR spectra recorded as a function of pH reflect again increasing number of nitrogen donors around the metal ions with increasing pH.…”

Section: At Two-fold Excess Of Ligand Over the Metal Ion Bis-complexesmentioning

confidence: 82%

“…However, the equilibrium constant of the process Zn 2+ + H 2 L = ZnH 2 L (log K = 6.58) is higher than the related value for histamine itself (log  101 = 5.15 [30]), or those of some {3N im } and {NH 2 ,2N im } coordinated complexes (log K = 5.1 [31] and 5.94 [29], respectively), indicating that additional binding sites should be taken into consideration. [12,34]. Therefore, during the last two processes the deprotonation of the Lys residues take place.…”

Section: Zinc(ii) Complexesmentioning

confidence: 99%

“…Recently, we studied the metal binding ability of the N-terminal histidine-rich fragment (H 2 N-HGDHMHNHDTK-OH) of this enzyme [12]. As a consequence of its highly versatile multidentate nature, this peptide binds zinc(II) and copper(II) with very high affinity (K D,Zn = 1.6×10 -9 M and K D,Cu = 5.0×10 -12 M at pH 7.4) and appears to be the strongest non-amide utilizing copper(II) and zinc (II) chelator among the His-rich peptides so far investigated, which supports the proposed copper(II) chaperoning role of the N-terminal His-rich region of H. ducreyi Cu,Zn SOD, and indicates similar function in the zinc(II) uptake, too [12].…”

Section: Introductionmentioning

confidence: 99%

“…Since the copper(II) complex of the H. ducreyi peptide formed in the neutral pH range has significant SOD-like activity [12], which may suggest multifunctional role of the copper(II)-bound N-terminal His-rich domain, this behavior has been studied for the presently studied complexes, too.…”

Section: Introductionmentioning

confidence: 99%

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On the possible roles of N-terminal His-rich domains of Cu,Zn SODs of some Gram-negative bacteria

Árus

Jancsó

Szunyogh

et al. 2012

Journal of Inorganic Biochemistry

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Harnessing the Flexibility of Peptidic Scaffolds to Control their Copper(II)‐Coordination Properties: A Potentiometric and Spectroscopic Study

Fragoso

Lamosa

Delgado

et al. 2013

Chemistry A European J

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Designing small peptides that are capable of binding Cu(2+) ions mainly through the side-chain functionalities is a hard task because the amide nitrogen atoms strongly compete for Cu(2+) ion coordination. However, the design of such peptides is important for obtaining biomimetic small systems of metalloenyzmes as well as for the development of artificial systems. With this in mind, a cyclic decapeptide, C-Asp, which contained three His residues and one Asp residue, and its linear derivative, O-Asp, were synthesized. The C-Asp peptide has two Pro-Gly β-turn-inducer units and, as a result of cyclization, and as shown by CD spectroscopy, its backbone is constrained into a more defined conformation than O-Asp, which is linear and contains a single Pro-Gly unit. A detailed potentiometric, mass spectrometric, and spectroscopic study (UV/Vis, CD, and EPR spectroscopy) showed that at a 1:1 Cu(2+)/peptide ratio, both peptides formed a major [CuHL](2+) species in the pH range 5.0-7.5 (C-Asp) and 5.5-7.0 (O-Asp). The corrected stability constants of the protonated species (log K*(CuH(O-Asp))=9.28 and log K*(CuH(C-Asp))=10.79) indicate that the cyclic peptide binds Cu(2+) ions with higher affinity. In addition, the calculated value of K(eff) shows that this higher affinity for Cu(2+) ions prevails at all pH values, not only for a 1:1 ratio but even for a 2:1 ratio. The spectroscopic data of both [CuHL](2+) species are consistent with the exclusive coordination of Cu(2+) ions by the side-chain functionalities of the three His residues and the Asp residue in a square-planar or square-pyramidal geometry. Nonetheless, although these data show that, upon metal coordination, both peptides adopt a similar fold, the larger conformational constraints that are present in the cyclic scaffold results in different behaviour for both [CuHL](2+) species. CD and NMR analysis revealed the formation of a more rigid structure and a slower Cu(2+)-exchange rate for [CuH(C-Asp)](2+) compared to [CuH(O-Asp](2+). This detailed comparative study shows that cyclization has a remarkable effect on the Cu(2+)-coordination properties of the C-Asp peptide, which binds Cu(2+) ions with higher affinity at all pH values, stabilizes the [CuHL](2+) species in a wider pH range, and has a slower Cu(2+)-exchange rate compared to O-Asp.

show abstract

Copper and zinc binding properties of the N-terminal histidine-rich sequence of Haemophilus ducreyi Cu,Zn superoxide dismutase

Cited by 36 publications

References 44 publications

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

Competition of zinc(II) with cadmium(II) or mercury(II) in binding to a 12-mer peptide

On the possible roles of N-terminal His-rich domains of Cu,Zn SODs of some Gram-negative bacteria

Harnessing the Flexibility of Peptidic Scaffolds to Control their Copper(II)‐Coordination Properties: A Potentiometric and Spectroscopic Study

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