Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa (Articolo in rivista)

Type

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

Label

• Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

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

• 10.1073/pnas.0607890103 (literal)

Alternative label

• Cascella, M; Magistrato, A; Tavernelli, I; Carloni, P; Rothlisberger, U (2006)
  Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa
  in Proceedings of the National Academy of Sciences of the United States of America
  (literal)

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

• Cascella, M; Magistrato, A; Tavernelli, I; Carloni, P; Rothlisberger, U (literal)

Pagina inizio

• 19641 (literal)

Pagina fine

• 19646 (literal)

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

• 103 (literal)

Rivista

• Proceedings of the National Academy of Sciences of the United States of America (Rivista)

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

• 52 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Ecole Polytech Fed Lausanne, Lab Computat Chem & Biochem, CH-1015 Lausanne, Switzerland; CNR, Natl Inst Phys Matter, Democritos Natl Simulat Ctr, I-34014 Trieste, Italy; Scuola Int Super Studi Avanzati, I-34014 Trieste, Italy (literal)

Titolo

• Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa (literal)

Abstract

• We have coupled hybrid quantum mechanics (density functional theory; Car-Parrinello)/molecular mechanics molecular dynamics simulations to a grand-canonical scheme, to calculate the in situ redox potential of the Cu2+ + e(-) -> Cu+ half reaction in azurin from Pseudomonas aeruginosa. An accurate description at atomistic level of the environment surrounding the metal-binding site and finite-temperature fluctuations of the protein structure are both essential for a correct quantitative description of the electronic properties of this system. We report a redox potential shift with respect to copper in water of 0.2 eV (experimental 0.16 eV) and a reorganization free energy lambda = 0.76 eV (experimental 0.6-0.8 eV). The electrostatic field of the protein plays a crucial role in fine tuning the redox potential and determining the structure of the solvent. The inner-sphere contribution to the reorganization energy is negligible. The overall small value is mainly due to solvent rearrangement at the protein surface. (literal)

Prodotto di

• Modelizzazione molecolare di sistemi biologici (MD.P06.026.001) (Modulo)

Autore CNR

• PAOLO CARLONI (Unità di personale esterno)
• ALESSANDRA MAGISTRATO (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• ALESSANDRA MAGISTRATO (Unità di personale interno)
• PAOLO CARLONI (Unità di personale esterno)

Prodotto

• Modelizzazione molecolare di sistemi biologici (MD.P06.026.001) (Modulo)

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

• Proceedings of the National Academy of Sciences of the United States of America (Rivista)

Insieme di parole chiave di

• Keywords of "Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa" (Insieme di parole chiave)