http://www.cnr.it/ontology/cnr/individuo/prodotto/ID271042
Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites (Articolo in rivista)
- Type
- Label
- Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.jinorgbio.2013.07.008 (literal)
- Alternative label
Á. Grenács, A. Kaluha, C. Kállay, V. Jószai, D. Sanna, I. Sóvágó (2013)
Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites
in Journal of inorganic biochemistry
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Á. Grenács, A. Kaluha, C. Kállay, V. Jószai, D. Sanna, I. Sóvágó (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.sciencedirect.com/science/article/pii/S0162013413001633 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4010 Debrecen, Hungary; Research Group of Homogeneous Catalysis and Reaction Mechanism, Hungarian Academy of Sciences, H-4010 Debrecen, Hungary; Istituto di Chimica Biomolecolare, CNR, Traversa La Crucca 3, 07040 Li Punti (SS), Italy (literal)
- Titolo
- Binary and ternary mixed metal complexes of terminally free peptides containing two different histidyl binding sites (literal)
- Abstract
- Copper(II), nickel(II) and zinc(II) complexes of the terminally free peptides AHAAAHG and AAHAAAHG have been studied by combined applications of potentiometric and various spectroscopic techniques, including UV-visible, CD and EPR for copper(II) and UV-visible, CD and NMR for nickel(II). It was found that the octapeptide AAHAAAHG can easily bind two equivalents of copper(II) or nickel(II) ions and the amino terminus was identified as the primary ligating site of the molecule. On the other hand, this peptide has a relatively low zinc(II) binding affinity. Mono- and di-nuclear copper(II) and nickel(II) complexes were also formed with the heptapeptide AHAAAHG but this peptide can effectively bind one equivalent of zinc(II) ions, too, with the involvement of the deprotonated amide nitrogen in zinc(II) binding. The enhanced stability of the [MH-1L] species of AHAAAHG was explained by the tridentate (NH2,N-,Nim) coordination of the amino terminus supported by the macrochelation of the internal histidyl residue. Mixed metal copper(II)-nickel(II) complexes were also formed with both peptides and copper(II) ions were coordinated to the amino terminal, while nickel(II) ions to the internal histidyl sites. (literal)
- Prodotto di
- Autore CNR
- Insieme di parole chiave
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Insieme di parole chiave di