Copper(II) complexes of amino acid derivatives of the bis(imidazol-2-yl)methyl residue. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Copper(II) complexes of amino acid derivatives of the bis(imidazol-2-yl)methyl residue. (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1039/B316813A (literal)

Alternative label

• Kàllay C., Cattari M., Sanna D., Vàrnagy K., Suli-Vargha H., Csàmpai A., Sòvàgò I., Micera G. (2004)
  Copper(II) complexes of amino acid derivatives of the bis(imidazol-2-yl)methyl residue.
  in New journal of chemistry (1987)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Kàllay C., Cattari M., Sanna D., Vàrnagy K., Suli-Vargha H., Csàmpai A., Sòvàgò I., Micera G. (literal)

Pagina inizio

• 727 (literal)

Pagina fine

• 734 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://pubs.rsc.org/en/Content/ArticleLanding/2004/NJ/b316813a (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 28 (literal)

Rivista

• New journal of chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Inorganic and Analytical Chemistry, University of Debrecen, P. O. Box 21, Debrecen, Hungary Department of Chemistry, University of Sassari, Via Vienna 2, Sassari, Italy Istituto C.N.R. di Chimica Biomolecolare, Sezione di Sassari, Trav. La Crucca 3 Reg. Baldinca, Sassari, Italy Research Group of Peptide Chemistry, Hungarian Academy of Sciences, P. O. Box 32, Budapest 112, Hungary Department of General and Inorganic Chemistry, Eötvös Loránd University, P. O. Box 32, Budapest 112, Hungary (literal)

Titolo

• Copper(II) complexes of amino acid derivatives of the bis(imidazol-2-yl)methyl residue. (literal)

Abstract

• Copper(II) complexes of amino acid derivatives of bis(imidazol-2-yl)methylamine (BIMA), ?-Asp-BIMA, ?-Glu-BIMA, ?-Glu-BIMA and ?-Ala-BIMA, were studied by potentiometric, UV-VIS and EPR techniques. The bis(imidazol-2-yl)methyl residue is the main binding site in strong acidic medium in all cases. The formation of ligand-bridged dinuclear [Cu2L2]2+ species was detected in an equimolar solution of ?-Asp-BIMA and ?-Glu-BIMA with binding of the N-terminal amino and carboxylate groups. The deprotonation of amide nitrogen takes place above pH 6 for the ligands containing an amide group in a chelatable position with terminal amino group (?-Asp-BIMA, ?-Glu-BIMA and ?-Ala-BIMA), resulting in the formation of dinuclear [Cu2H-2L2] species with imidazole bridging. For these 3 ligands, deprotonation of the pyrrole-type nitrogen was observed and the existence of a trinuclear species [Cu3H-4L2] was assumed in alkaline solution. This species contains negatively charged imidazolato bridges. (literal)

Prodotto di

• Institute of biomolecular chemistry (ICB) (Istituto)
• Caratterizzazione di complessi metallici formati da proteine coinvolte in patologie correlate al disordine conformazionale proteico. (PM.P01.004.002) (Modulo)

Autore CNR

• DANIELE SANNA (Unità di personale interno)

Incoming links:

Autore CNR di

• DANIELE SANNA (Unità di personale interno)

Prodotto

• Institute of biomolecular chemistry (ICB) (Istituto)
• Caratterizzazione di complessi metallici formati da proteine coinvolte in patologie correlate al disordine conformazionale proteico. (PM.P01.004.002) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• New journal of chemistry (Rivista)