1H NMR structural characterization of the cytochrome c modifications in a micellar environment

Autor: J. D. De Certaines, E. Le Rumeur, G. Simonneaux, Soizic Chevance, Arnaud Bondon
Přispěvatelé: Institut des Sciences Chimiques de Rennes (ISCR), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), SIM, Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2003
Předmět:
MESH: Oxidation-Reduction
Ligands
Ferric Compounds
Biochemistry
chemistry.chemical_compound
MESH: Spectrophotometry
Ultraviolet
MESH: Nuclear Magnetic Resonance
Biomolecular
MESH: Ligands
MESH: Animals
heme
Heme
biology
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Structural Biology [q-bio.BM]
Chemistry
Cytochrome c
MESH: Micelles
Cytochromes c
Sodium Dodecyl Sulfate
MESH: Cytochromes c
MESH: Ferrous Compounds
cytochrome c
MESH: Heme
Proton NMR
Thermodynamics
protein-membrane interaction
MESH: Ferric Compounds
Protons
MESH: Thermodynamics
Oxidation-Reduction
Two-dimensional nuclear magnetic resonance spectroscopy
medicine.drug
MESH: Sodium Dodecyl Sulfate
micelles
Cyanide
Inorganic chemistry
Adduct
Electron Transport
Electron transfer
medicine
Animals
Ferrous Compounds
Horses
MESH: Electron Transport
MESH: Horses
Nuclear Magnetic Resonance
Biomolecular
NMR
Crystallography
13. Climate action
biology.protein
Ferric
Spectrophotometry
Ultraviolet
MESH: Protons
Zdroj: Biochemistry
Biochemistry, American Chemical Society, 2003, 42 (51), pp.15342-51. ⟨10.1021/bi035044+⟩
Biochemistry, 2003, 42 (51), pp.15342-51. ⟨10.1021/bi035044+⟩
ISSN: 0006-2960
1520-4995
DOI: 10.1021/bi035044+⟩
Popis: International audience; The interaction of cytochrome c with micelles of sodium dodecyl sulfate was studied by proton NMR spectroscopy. The protein/micelles ratio was found to be crucial in controlling the extent of the conformational changes in the heme crevice. Over a range of ratios between 1:30 and 1:60, the NMR spectra of the ferric form display no paramagnetic signals due to a moderately fast exchange between intermediate species on the NMR time scale. This is consistent with an interconversion of bis-histidine derivatives (His18-Fe-His26 and His18-Fe-His33). Further addition of micelles induces a high-spin species that is proposed to involve pentacoordinated iron. The resulting free binding site, also encountered in the ferrous form, is used to complex exogenous ligands such as cyanide or carbon monoxide. Attribution of the heme methyls was performed by means of exchange spectroscopy through ligand exchange or electron transfer. The heme methyl shift pattern of the micellar cyanocytochrome in the ferric low spin form is different from the pattern of both the native and the cyanide cytochrome c adduct, in the absence of micelles, reflecting a complete change of the heme electronic structure. Analysis of the electron self-exchange reaction between the two redox states of the micellar cyanocytochrome c yields a rate constant of 2.4 x 10(4) M(-1) s(-1) at 298 K, which is surprisingly close to the value observed in the native protein.
Databáze: OpenAIRE
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