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M Chergui

Publications and source records attributed to M Chergui.

12 recordsLinked to original sources
PubMed2006

Photexcitation of aqueous ruthenium(II)-tris-(2,2'-bipyridine) with high-intensity femtosecond laser pulses.

We report a femtosecond pump-probe study on the photochemistry of concentrated aqueous solutions of [RuII(bpy)3]2+, as a function of pump power (up to 2 TW/cm2) at 400 nm excitation. The transient absorption spectra in the 345-660 nm range up to 1 ns time delay enable the observation of the following photoproducts: the triplet 3MLCT (metal-to-ligand-charge-transfer) excited state, the reduced form [RuII(bpy)3]+, the oxidized species [RuIII(bpy)3]3+, and the solvated electron e(aq). The 3MLCT state is formed within the excitation pulse and undergoes vibrational relaxation in 3-5 ps, as evidenced by the shift of the ligand-centered (LC) absorption band below 400 nm. Even at the highest pump powers, the majority of e(aq) originates from multiphoton ionization of [RuII(bpy)3]2+ and not from the solvent, generating [RuIII(bpy)3]3+ as a byproduct. At 10 ps time delay, the total concentration of the three product species is balanced by the depleted concentration of [RuII(bpy)3]2+, even at the highest fluences used, indicating that no further reaction products significantly contribute to the overall photochemistry. On the 100 ps time scale, most probably diffusion-controlled reduction of ground-state [RuII(bpy)3]2+ by solvated electrons occurs, next to recombination between e(aq) and [RuIII(bpy)3]3+.

Journal Article↗
PubMed2006

The ultrafast structural response of solid parahydrogen: a complementary experimental/simulation investigation.

We present a complete characterization, based on femtosecond pump-probe spectroscopy and molecular dynamics simulations, of the ultrafast dynamics of electronic bubble formation in solid parahydrogen upon impulsive excitation of impurity-doped sites, which correlate with the lowest Rydberg state of the NO impurity. The high temporal resolution of the experiment allows us to identify three time scales in the structural dynamics. A first ultrafast expansion (<150 fs), associated with the release of approximately 80% of the excess energy available to the system after excitation, is accompanied by a transient narrowing of the spatial distribution of the first shell of H2 molecules around the impurity. In a subsequent stage (up to approximately 800 fs), the cavity expansion slows down, and energy starts to flow irreversibly into the crystal. Finally, the lattice undergoes a slow structural reorganization at the impurity site (5-10 ps). A weak low-frequency recurrence, probably associated with an elastic response of the crystal, is observed at approximately 10 ps. The absence of polarization dependence indicates that the dynamics is largely dominated by translational (radial) motions of the molecules surrounding NO and not by the rotational motion of the impurity. Molecular dynamics simulations with temperature corrections, to mimic zero-point fluctuations, fully support the experimental results and show that the bubble model is suited to describe the dynamics of the system. It appears that the response of the medium around the impurity at short times is typical of a liquid solvent rather than that of a solid.

Journal Article↗
PubMed2006

Sulfide-binding hemoglobins: Effects of mutations on active-site flexibility.

The dynamics of Hemoglobin I (HbI) from the clam Lucina pectinata, from wild-type sperm whale (SW) myoglobin, and from the L29F/H64Q/V68F triple mutant of SW, both unligated and bound to hydrogen sulfide (H2S), have been studied in molecular dynamics simulations. Features that account for differences in H2S affinity among the three have been examined. Our results verify the existence of an unusual heme rocking motion in unligated HbI that can promote the entrance of large ligands such as H2S. The FQF-mutant partially reproduces the amplitude and relative orientation of the motion of HbI's heme group. Therefore, besides introducing favorable electrostatic interactions with H2S, the three mutations in the distal pocket change the dynamic properties of the heme group. The active-site residues Gln-64(E7), Phe-43(CD1), and His-93(F8) are also shown to be more flexible in unligated HbI than in FQF-mutant and SW. Further contributions to H2S affinity come from differences in hydrogen bonding between the heme propionate groups and nearby amino acid residues.

Amino Acid Substitution↗
PubMed2006

Absorption spectroscopy of three-dimensional bacteriorhodopsin crystals at cryogenic temperatures: effects of altered hydration.

A comparative study of absorption spectroscopy at 100 K has been performed on three-dimensional crystals of bacteriorhodopsin extracted from a lipidic cubic phase and on native purple membrane. A modified microspectrophotometer has been designed which yields absorption data with a high signal-to-noise ratio and remarkable reproducibility. Excellent agreement of the absorption spectra of the three-dimensional crystals and the purple membrane is observed provided that a rigorous crystal-handling procedure is followed. This result supports the equivalence of the protein structure in both the cubic phase crystals and the native purple membrane. On the other hand, it is shown that dramatic deviations of the crystal spectrum can be induced by minor changes in the extraction method. Exposure to air at room temperature can lead within a short time to an irreversible dehydration manifested by a distinct species with an absorption maximum at 500 nm. Exposure of the crystals to a buffer with lower ionic strength than the crystallization solution produces a different spectral form with an absorption maximum at 477 nm, which was assigned to a distorted protein conformation induced by osmotic stress. The extreme sensitivity of these crystals to experimental conditions is relevant for X-ray structural studies, in particular as different experimental treatments are implemented to trap the intermediates of the protein's photocycle.

Bacteriorhodopsins↗
PubMed2006

Insights into excited-state and isomerization dynamics of bacteriorhodopsin from ultrafast transient UV absorption.

A visible-pump/UV-probe transient absorption is used to characterize the ultrafast dynamics of bacteriorhodopsin with 80-fs time resolution. We identify three spectral components in the 265- to 310-nm region, related to the all-trans retinal, tryptophan (Trp)-86 and the isomerized photoproduct, allowing us to map the dynamics from reactants to products, along with the response of Trp amino acids. The signal of the photoproduct appears with a time delay of approximately 250 fs and is characterized by a steep rise ( approximately 150 fs), followed by additional rise and decay components, with time scales characteristic of the J intermediate. The delayed onset and the steep rise point to an impulsive formation of a transition state on the way to isomerization. We argue that this impulsive formation results from a splitting of a wave packet of torsional modes on the potential surface at the branching between the all-trans and the cis forms. Parallel to these dynamics, the signal caused by Trp response rises in approximately 200 fs, because of the translocation of charge along the conjugate chain, and possible mechanisms are presented, which trigger isomerization.

Bacteriorhodopsins↗
PubMed2005

Probing the ultrafast charge translocation of photoexcited retinal in bacteriorhodopsin.

The ultrafast evolution of the electric field within bacteriorhodopsin was measured by monitoring the absorption changes of a tryptophan residue after excitation of retinal. The Trp absorption decreases within the first 200 femtoseconds and then recovers on time scales typical for retinal isomerization and vibrational relaxation. A model of excitonic coupling between retinal and tryptophans shows that the signal reflects a gradual rise of the retinal difference dipole moment, which precedes and probably drives isomerization. The results suggest an intimate connection between the progressive dipole moment change and the retinal skeletal changes reported over the same time scale.

Bacteriorhodopsins↗
PubMed2005

Lattice response of quantum solids to an impulsive local perturbation.

The lattice response of solid para-H2 to an impulsive electronic excitation was studied using femtosecond pump-probe spectroscopy. The evolution of an electronic bubble in the crystal, created upon excitation of the A(3ssigma) Rydberg state of an NO impurity, was followed in real time, with a resolution of 100 fs. The experimental results, interpreted in connection with molecular dynamics simulations with quantum corrections, indicate the presence of three stages in the dynamics: a sub-100 fs "adiabatic" phase, a 0.5-1 ps phase, corresponding to the interaction of the first with the next shells driven by the bubble expansion, and a 5 ps phase, corresponding to a slow rearrangement of the environment surrounding the impurity. These findings indicate that the lattice response in solid para-H2 resembles that of a liquid.

Journal Article↗
PubMed2002

Femtosecond and picosecond fluorescence of native bacteriorhodopsin and a nonisomerizing analog.

The spectrally and temporally resolved fluorescence properties of native bacteriorhodopsin (bR) and bR reconstituted with a nonisomerizing analog of the retinal Schiff base (bR5.12) are examined. The first attempt to experimentally monitor the excited state relaxation processes in both type of pigments using ultrafast fluorescence spectroscopy is reported. The fluorescence is emitted from retinal molecules in an all-trans configuration. Substantial energy relaxation involves very fast intramolecular and intermolecular vibrational modes and these are shown to occur on a time scale faster than isomerization. The possible contribution of dielectric interaction between the retinal Schiff base and the protein environment for the excited state energy relaxation is discussed.

Bacteriorhodopsins↗
PubMedDate not supplied

[Study of symbiotic, serological and antibiotic resistance characteristics of different Rhizobium cicerii strains].

The symbiotic performance of 24 isolates of Rhizobium Cicerii, collected from different Tunisien soils, were studied in a growth room and compared to the performance of two international strains (Som and 43). The antibiotic and serologic tests showed a large biogenetic diversity among the different isolates. Three serogroups gathering 18 isolates have been identified. Monchar strain (isolat 12) was shown to be resistant to all the six different antibiotic used. The standard strain 43 produced the greatest number of nodules and the best nitrogen yield in association with "Amdoun" roots, whereas the Menzel bouzelfa isolate brought about the best nitrogen yield in association with "Amdoun" and thus was the most efficient. An interesting result, consisted on the existence of a significant correlation (r = 0.67) between streptomycin resistance of the isolates and their capacity of nodule initiation (infectivity).

Drug Resistance, Microbial↗