A variety of copper(lI) complexes with di-, tri- and tetra-peptides containing only glycine residues (GG, GGG and GGGG) and others containing a histidyl residue in different positions (HGG, GHG, GGH and GGHG) have been investigated. EPR parameters obtained by extensive use of computer simulation of spectra lead to reliable spin Hamiltonian EPR parameters at both room temperature and in frozen solution. The molecular orbital coefficients computed from the anisotropic EPR data and the d-d electronic energies are used to characterize different arrangements of the complexes. Estimation of the scavenger activity of the complexes due to the particular environment created by the ligands around copper is discussed in the frame of the structure-activity relationship.

Pogni, R., Baratto, M.C., Busi, E., Basosi, R. (1999). EPR and O2- Scavenger Activity: Cu(II)-Peptide Complexes as Superoxide Dismutase Models. JOURNAL OF INORGANIC BIOCHEMISTRY, 73, 157-165 [10.1016/S0162-0134(99)00012-4].

EPR and O2- Scavenger Activity: Cu(II)-Peptide Complexes as Superoxide Dismutase Models

POGNI, REBECCA;BARATTO, MARIA CAMILLA;BUSI, ELENA;BASOSI, RICCARDO
1999-01-01

Abstract

A variety of copper(lI) complexes with di-, tri- and tetra-peptides containing only glycine residues (GG, GGG and GGGG) and others containing a histidyl residue in different positions (HGG, GHG, GGH and GGHG) have been investigated. EPR parameters obtained by extensive use of computer simulation of spectra lead to reliable spin Hamiltonian EPR parameters at both room temperature and in frozen solution. The molecular orbital coefficients computed from the anisotropic EPR data and the d-d electronic energies are used to characterize different arrangements of the complexes. Estimation of the scavenger activity of the complexes due to the particular environment created by the ligands around copper is discussed in the frame of the structure-activity relationship.
Pogni, R., Baratto, M.C., Busi, E., Basosi, R. (1999). EPR and O2- Scavenger Activity: Cu(II)-Peptide Complexes as Superoxide Dismutase Models. JOURNAL OF INORGANIC BIOCHEMISTRY, 73, 157-165 [10.1016/S0162-0134(99)00012-4].
File in questo prodotto:
File Dimensione Formato  
JIB_1999.pdf

non disponibili

Tipologia: Post-print
Licenza: NON PUBBLICO - Accesso privato/ristretto
Dimensione 687.4 kB
Formato Adobe PDF
687.4 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/23439
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo