A bis-histidine-ligated unfolded cytochrome c immobilized on anionic SAM shows pseudo-peroxidase activity (Articolo in rivista)

Type

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

Label

• A bis-histidine-ligated unfolded cytochrome c immobilized on anionic SAM shows pseudo-peroxidase activity (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.elecom.2011.10.021 (literal)

Alternative label

• Ranieri A, G. Battistuzzi, M. Borsari, CA Bortolotti, G Di Rocco, S Monari, M Sola (2012)
  A bis-histidine-ligated unfolded cytochrome c immobilized on anionic SAM shows pseudo-peroxidase activity
  in Electrochemistry communications
  (literal)

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

• Ranieri A, G. Battistuzzi, M. Borsari, CA Bortolotti, G Di Rocco, S Monari, M Sola (literal)

Pagina inizio

• 29 (literal)

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

• 14 (literal)

Rivista

• Electrochemistry communications (Rivista)

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

• Department of Chemistry, University of Modena and Reggio Emilia, via Campi 183, 41125 Modena, Italy; CNR-INFM National Center nanoStructures and bioSystems at Surfaces, S3, Via Campi 213/A, I-41125 Modena, Italy (literal)

Titolo

• A bis-histidine-ligated unfolded cytochrome c immobilized on anionic SAM shows pseudo-peroxidase activity (literal)

Abstract

• Urea-unfolded yeast iso-1-cytochrome c electrostatically adsorbed on a gold electrode coated with an anionic self-assembled monolayer yields a heme-mediated electrocatalytic reduction of H2O2 (pseudo-peroxidase activity). Under the same conditions, native cytochrome c is inactive. In the unfolded protein, the Met80 heme iron ligand is replaced by a histidine residue yielding a bis-His-ligated form. H2O2 electrocatalysis occurs with an efficient mechanism likely involving direct H2O2 interaction with the iron(II) center and formation of a transient ferryl group. Comparison of the catalytic activity of a few urea-unfolded single and double Lys-to-Ala variants shows that the kinetic affinity of H2O2 for the heme iron and kcat of the bis-His-ligated form are strongly affected by the geometry of protein adsorption, controlled by specific surface lysine residues. (literal)

Prodotto di

• Nanobiosistemi (MD.P06.010.002) (Modulo)

Autore CNR

• Marco Sola (Persona)

Incoming links:

Autore CNR di

• Marco Sola (Persona)

Prodotto

• Nanobiosistemi (MD.P06.010.002) (Modulo)

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

• Electrochemistry communications (Rivista)