Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Jacqueline Bergès"'
Publikováno v:
Structural Chemistry. 31:719-730
The first steps of the oxidation process of amino acid methionine (Met, CAS 63-68-3) by •OH radicals, leading to Met-OH• adduct and then to Met radical cation, were investigated theoretically over the last few years considering the aqueous enviro
Publikováno v:
Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2017, 121 (40), pp.9321-9330. ⟨10.1021/acs.jpcb.7b05796⟩
Journal of Physical Chemistry B, 2017, 121 (40), pp.9321-9330. ⟨10.1021/acs.jpcb.7b05796⟩
Journal of Physical Chemistry B, American Chemical Society, 2017, 121 (40), pp.9321-9330. ⟨10.1021/acs.jpcb.7b05796⟩
Journal of Physical Chemistry B, 2017, 121 (40), pp.9321-9330. ⟨10.1021/acs.jpcb.7b05796⟩
International audience; Oxidative stress of sulfur-containing biological molecules in aqueous environments may lead to the formation of adduct intermediates that are too short-lived to be experimentally detectable. In this study we have modeled the s
Publikováno v:
The Journal of Physical Chemistry B. 120:9875-9886
Oxidation of peptides or proteins by the OH(•) radicals produced by pulse radiolysis yields species identified by their absorption spectra in the UV-visible domain. However, the case of methionine (Met) in peptides is complex because its oxidation
Publikováno v:
Radiation Physics and Chemistry
Radiation Physics and Chemistry, 2016, ⟨10.1016/j.radphyschem.2016.05.007⟩
Radiation Physics and Chemistry, Elsevier, 2016, ⟨10.1016/j.radphyschem.2016.05.007⟩
Radiation Physics and Chemistry, 2016, ⟨10.1016/j.radphyschem.2016.05.007⟩
Radiation Physics and Chemistry, Elsevier, 2016, ⟨10.1016/j.radphyschem.2016.05.007⟩
International audience; Methionine is an essential amino acid, unfortunately prone to oxidation. The mechanism of its oxidation by • OH radicals has been studied for more than 40 years and still remains misunderstood. We have reinvestigated the oxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2132d7458c01226ce70711a5f2920252
https://hal.sorbonne-universite.fr/hal-01320731
https://hal.sorbonne-universite.fr/hal-01320731
Publikováno v:
Angewandte Chemie. 122:7602-7605
We report here the first crystallographic evidence for a hydrogen-bonding-like interaction between a water molecule and a d8 metal ion, based on neutron diffraction. According to our HF and MP2 calculations, the interaction is almost entirely dispers
Publikováno v:
International Journal of Quantum Chemistry. 111:1143-1151
Oxidation of peptides and proteins by •OH radicals produced in oxidative stress or in radiotherapy, accidental irradiations, etc., is well known to form oxidative metabolites that are responsible for numerous diseases including neurodegenerative pa
Autor:
Chantal Houée-Levin, Jacqueline Bergès
Publikováno v:
Research on Chemical Intermediates. 35:421-430
Protein sulphur functions can host a single electron on sulphur atoms in redox processes linking thiols to disulphides. However, experimental results have shown that the single electron can also reside on carbon atoms leading to protein damage. We ha
Publikováno v:
Chemical Physics Letters. 467:164-169
Small models of radical cations of methionine-containing dipeptides, which are stabilized by formation of two-centre three-electron (2c–3e) S∴X bonds (X = S, N and O), were investigated at the BH&HLYP/6-31G(d) level and by means of topological to
Autor:
Jacqueline Bergès, Chantal Houée-Levin
Publikováno v:
Radiation Physics and Chemistry. 77:1286-1289
The protein sulfur functions have numerous cellular fundamental roles. They are in charge of the maintenance of the cellular reduction potential, which in turn governs gene expression. In addition, the redox cycling of disulfide/thiol functions has a
Publikováno v:
The Journal of Physical Chemistry B. 112:5774-5787
Thioredoxin controls the intracellular redox potential through a disulfide/dithiol couple. Under conditions of oxidative stress, this protein functions via one-electron exchange, in which formation of the disulfide radical anion occurs. Combined quan