Mid- and Far-Infrared Marker Bands of the ...
Type de document :
Compte-rendu et recension critique d'ouvrage
DOI :
Titre :
Mid- and Far-Infrared Marker Bands of the Metal Coordination Sites of the Histidine Side Chains in the Protein Cu,Zn-Superoxide Dismutase
Auteur(s) :
Xerri, Bertrand [Auteur]
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier [ICGM ICMMM]
Petitjean, Hugo [Auteur]
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier [ICGM ICMMM]
Dupeyrat, François [Auteur]
Aix Marseille Université [AMU]
Interactions Protéine Métal [IPM]
Flament, Jean-Pierre [Auteur]
Laboratoire de Physique des Lasers, Atomes et Molécules - UMR 8523 [PhLAM]
Lorphelin, Alain [Auteur]
Service de Biochimie et Toxicologie Nucléaire [SBTN]
Vidaud, Claude [Auteur]
Service de Biochimie et Toxicologie Nucléaire [SBTN]
Berthomieu, C. [Auteur correspondant]
Interactions Protéine Métal [IPM]
Aix Marseille Université [AMU]
Berthomieu, Dorothée [Auteur correspondant]
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier [ICGM ICMMM]
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier [ICGM ICMMM]
Petitjean, Hugo [Auteur]
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier [ICGM ICMMM]
Dupeyrat, François [Auteur]
Aix Marseille Université [AMU]
Interactions Protéine Métal [IPM]
Flament, Jean-Pierre [Auteur]
Laboratoire de Physique des Lasers, Atomes et Molécules - UMR 8523 [PhLAM]
Lorphelin, Alain [Auteur]
Service de Biochimie et Toxicologie Nucléaire [SBTN]
Vidaud, Claude [Auteur]
Service de Biochimie et Toxicologie Nucléaire [SBTN]
Berthomieu, C. [Auteur correspondant]
Interactions Protéine Métal [IPM]
Aix Marseille Université [AMU]
Berthomieu, Dorothée [Auteur correspondant]
Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier [ICGM ICMMM]
Titre de la revue :
European Journal of Inorganic Chemistry
Pagination :
4650–4659
Éditeur :
Wiley-VCH Verlag
Date de publication :
2014-09
ISSN :
1434-1948
Mot(s)-clé(s) en anglais :
Enzyme models
Metalloenzymes
IR spectroscopy
Coordination modes
Density functional calculations
Metalloenzymes
IR spectroscopy
Coordination modes
Density functional calculations
Discipline(s) HAL :
Chimie/Chimie de coordination
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biophysique
Chimie/Chimie théorique et/ou physique
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biophysique
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Vibrational spectroscopy gives important information on the properties of ligand and metal–ligand bonds in metalloenzymes. Infrared spectroscopy is appealing for the study of metal active sites that are not amenable to ...
Lire la suite >Vibrational spectroscopy gives important information on the properties of ligand and metal–ligand bonds in metalloenzymes. Infrared spectroscopy is appealing for the study of metal active sites that are not amenable to Raman spectroscopy. We present a combined experimental and theoretical approach to analyze the mid- and far-IR spectra of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) as a probe of the histidine ligands. This metalloenzyme provides a unique model to identify specific IR signatures of metal–histidine coordination and to study their alterations as a function of the metal (copper/zinc), the copper valence state (+I/+II), the histidine coordination mode (Nτ and Nπ) and the histidine protonation state. DFT calculations combined with normal mode descriptions from potential energy distribution calculations were performed on two slightly different cluster models. Differences in the constraints at the side chain of one histidine Cu ligand sensibly modify the geometric parameters and vibrational properties. Electrochemically induced FTIR difference spectroscopy provided mid- and far-IR fingerprint spectra of the Cu protein in aqueous media that are sensitive to the redox state of the Cu centre at the active site. Comparisons of the DFT predictions with the experimental IR modes of the histidine ligands at the Cu,Zn-SOD active site showed that useful mid-IR markers of histidine Nτ and Nπ coordination were predicted with good accuracy. The DFT analysis further demonstrated a link between the ν(C4–C5) mode frequency of His46 and the specific properties of the His46–Cu bond in Cu,Zn-SOD. A combined theoretical and experimental approach on samples in H2O and 2H2O or 15N-labelled samples identified the contributions from the histidine side chain modes in the 669–629 cm–1 region.Lire moins >
Lire la suite >Vibrational spectroscopy gives important information on the properties of ligand and metal–ligand bonds in metalloenzymes. Infrared spectroscopy is appealing for the study of metal active sites that are not amenable to Raman spectroscopy. We present a combined experimental and theoretical approach to analyze the mid- and far-IR spectra of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) as a probe of the histidine ligands. This metalloenzyme provides a unique model to identify specific IR signatures of metal–histidine coordination and to study their alterations as a function of the metal (copper/zinc), the copper valence state (+I/+II), the histidine coordination mode (Nτ and Nπ) and the histidine protonation state. DFT calculations combined with normal mode descriptions from potential energy distribution calculations were performed on two slightly different cluster models. Differences in the constraints at the side chain of one histidine Cu ligand sensibly modify the geometric parameters and vibrational properties. Electrochemically induced FTIR difference spectroscopy provided mid- and far-IR fingerprint spectra of the Cu protein in aqueous media that are sensitive to the redox state of the Cu centre at the active site. Comparisons of the DFT predictions with the experimental IR modes of the histidine ligands at the Cu,Zn-SOD active site showed that useful mid-IR markers of histidine Nτ and Nπ coordination were predicted with good accuracy. The DFT analysis further demonstrated a link between the ν(C4–C5) mode frequency of His46 and the specific properties of the His46–Cu bond in Cu,Zn-SOD. A combined theoretical and experimental approach on samples in H2O and 2H2O or 15N-labelled samples identified the contributions from the histidine side chain modes in the 669–629 cm–1 region.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
Projet ANR :
Source :
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