EPR characterisation of the ferrous nitrosyl complex formed within the oxygenase domain of NO synthase

Autor: Santolini , J., Maréchal , Amandine, Boussac , Alain, Dorlet , Pierre
Přispěvatelé: Stress Oxydants et Détoxication ( LSOD ), Département Biochimie, Biophysique et Biologie Structurale ( B3S ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), French Infrastructure for Integrated Structural Biology (FRISBI), ANR-10-INSB-05-01,FRISBI,French Infrastructure for Integrated Structural Biology, Stress Oxydants et Détoxication (LSOD), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010)
Jazyk: angličtina
Rok vydání: 2013
Předmět:
MESH: Myoglobin
MESH : Recombinant Proteins
Nitric Oxide Synthase Type II
[CHIM.INOR]Chemical Sciences/Inorganic chemistry
MESH : Coordination Complexes
Nitric Oxide
[ CHIM ] Chemical Sciences
Substrate Specificity
MESH: Recombinant Proteins
MESH: Protein Structure
Tertiary
MESH: Coordination Complexes
Coordination Complexes
MESH : Ferrous Compounds
[CHIM]Chemical Sciences
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Ferrous Compounds
nitrosyl complexes
MESH : Temperature
[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry
Molecular Biology
MESH : Isoenzymes
MESH : Substrate Specificity
Myoglobin
digestive
oral
and skin physiology
Electron Spin Resonance Spectroscopy
Temperature
MESH : Bacillus subtilis
[ CHIM.INOR ] Chemical Sciences/Inorganic chemistry
MESH: Bacillus subtilis
Full Papers
MESH : Nitric Oxide Synthase Type II
MESH: Temperature
Recombinant Proteins
MESH: Ferrous Compounds
Protein Structure
Tertiary
heme proteins
Isoenzymes
MESH : Electron Spin Resonance Spectroscopy
MESH : Nitric Oxide
MESH: Nitric Oxide
MESH: Isoenzymes
MESH: Electron Spin Resonance Spectroscopy
MESH: Substrate Specificity
MESH: Nitric Oxide Synthase Type II
NO-synthases
MESH : Protein Structure
Tertiary
Bacillus subtilis
EPR spectroscopy
MESH : Myoglobin
Zdroj: ChemBioChem
ChemBioChem, Wiley-VCH Verlag, 2013, 14 (14), pp.1852-7. 〈10.1002/cbic.201300233〉
Chembiochem
ChemBioChem, 2013, 14 (14), pp.1852-7. ⟨10.1002/cbic.201300233⟩
ChemBioChem, Wiley-VCH Verlag, 2013, 14 (14), pp.1852-7. ⟨10.1002/cbic.201300233⟩
ISSN: 1439-4227
1439-7633
DOI: 10.1002/cbic.201300233〉
Popis: International audience; Nitric oxide is produced in mammals by a class of enzymes called NO synthases (NOSs). It plays a central role in cellular signalling but also has deleterious effects, as it leads to the production of reactive oxygen and nitrogen species. NO forms a relatively stable adduct with ferrous haem proteins, which, in the case of NOS, is also a key catalytic intermediate. Despite extensive studies on the ferrous nitrosyl complex of other haem proteins (in particular myoglobin), little characterisation has been performed in the case of NOS. We report here a temperature-dependent EPR study of the ferrous nitrosyl complex of the inducible mammalian NOS and the bacterial NOS-like protein from Bacillus subtilis. The results show that the overall behaviours are similar to those observed for other haem proteins, but with distinct ratios between axial and rhombic forms in the case of the two NOS proteins. The distal environment appears to control the existence of the axial form and the evolution of the rhombic form.
Databáze: OpenAIRE
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