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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Varnagy, K. | en |
| dc.contributor.author | Szabo, J. | en |
| dc.contributor.author | Sovago I | en |
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.contributor.author | Sanna, D. | en |
| dc.contributor.author | Micera, G. | en |
| dc.date.accessioned | 2015-11-24T16:57:56Z | - |
| dc.date.available | 2015-11-24T16:57:56Z | - |
| dc.identifier.issn | 1472-7773 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10635 | - |
| dc.rights | Default Licence | - |
| dc.subject | nuclear-magnetic-resonance | en |
| dc.subject | glycylglycyl-l-histidine | en |
| dc.subject | metal-ion complexes | en |
| dc.subject | imidazole nitrogens | en |
| dc.subject | angiotensin-ii | en |
| dc.subject | transport site | en |
| dc.subject | serum-albumin | en |
| dc.subject | amino | en |
| dc.subject | oligopeptides | en |
| dc.subject | proton | en |
| dc.title | Equilibrium and structural studies on copper(II) complexes of tetra-, penta- and hexa-peptides containing histidyl residues at the C-termini | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://000085350300007 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2000 | - |
| heal.abstract | The stoichiometry, stability constants and solution structure of the complexes formed in the reaction of copper(II) with oligopeptides containing histidyl residues at the C-termini (Gly(3)His, Gly(4)His and Gly(5)His) have been determined by potentiometric, UV-VIS and EPR spectroscopic methods. The formation of the species [CuHL](2+), [CuL](+), [CuH(-1)L], [CuH(-2)L](-) and [CuH(-3)L](2-) was detected in all cases. Binding modes of the species [CuL](+), [CuH(-1)L] and [CuH(-2)L](-) were characterized by the metal ion co-ordination of the terminal amino group, carbonyl oxygen or one or two deprotonated amide nitrogens in joined five-membered chelates from the N-termini, while the fourth co-ordination site of the metal ion was occupied by nitrogen donors of imidazole in the form of a macrochelate. The stability of the macrochelate was decreased upon increasing the length of the peptide molecule. For the penta- and hexa-peptides the species [CuH(-3)L](2-) was characterized as a 4N-complex with equatorial co-ordination of the terminal amino group and subsequent three deprotonated amide nitrogens, with unco-ordinated imidazolyl residues, while a 5N-species was suggested to form for Gly(3)His with axial interaction of the imidazole-N donor atom. Copper(II) complexes of Gly(2)His and pentaglycine were also investigated for reliable comparison. | en |
| heal.journalName | Journal of the Chemical Society-Dalton Transactions | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Malandrinos-2000-Equilibrium and structural studies.pdf | 126.22 kB | Adobe PDF | View/Open Request a copy |
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