Publications

2006

• Measuring the dynamics of circular dichroism in a pump-probe experiment with a Babinet-Soleil compensator
  
  • Niezborala Claire
  • Hache François
  Journal of the Optical Society of America B, Optical Society of America, 2006, 23 (11), pp.2418. Circular dichroism contains rich information on the conformation of molecules and, in particular, of biomolecules, and measuring its variation in a pump-probe experiment is very promising but also very challenging. We propose a new technique to measure pump-induced variation of the circular dichroism, which is based on the measurement of the probe ellipticity and its variation with the pump. This technique has the advantage that it does not require modulation of the probe polarization, which allows modulation of the pump intensity. We show theoretically and demonstrate experimentally that this technique is very sensitive and user friendly. We also show that it can be used to measure pump-induced change in the optical rotation, allowing for a complete characterization of pump-induced optical activity. Cop. 2006 Optical Society of America. (10.1364/JOSAB.23.002418)
  DOI : 10.1364/JOSAB.23.002418
• Parametric cascade downconverter for intense ultrafast mid-infrared generation beyond the Manley-Rowe limit
  
  • Fraser James M.
  • Ventalon Cathie
  Applied optics, Optical Society of America, 2006, 45 (17), pp.4109-4113. We propose a scheme to generate intense, ultrafast mid-infrared pulses with conversion efficiencies exceeding the upper bound for single-stage difference-frequency mixing as predicted by the Manley-Rowe relations. Finite-element fast Fourier transform simulations of the mixing process show that the parametric cascade downconverter generates 1.7 times more photons (at 10 μm ) than in the initial pump pulse (center wavelength of 1.48 μm , duration of 130 fs , and pulse energy of 50 μJ ), with negligible pulse spatial and temporal distortion. © 2006 Optical Society of America (10.1364/AO.45.004109)
  DOI : 10.1364/AO.45.004109
• Hydrophobic distal pocket affects NO-heme geminate recombination dynamics in dehaloperoxidase and H64V myoglobin
  
  • Franzen S.
  • Jasaitis Audrius
  • Belyea J.
  • Brewer S.
  • Casey Romain
  • Macfarlane A.
  • Martin Jean-Louis
  • Stanley R.
  • Vos Marten H.
  Journal of Physical Chemistry B, American Chemical Society, 2006, 110 (29), pp.14483. The recombination dynamics of NO with dehaloperoxidase ( DHP) from Amphitrite ornata following photolysis were measured by femtosecond time- resolved absorption spectroscopy. Singular value decomposition ( SVD) analysis reveals two important basis spectra. The first SVD basis spectrum reports on the population of photolyzed NO molecules and has the appearance of the equilibrium difference spectrum between the deoxy and NO forms of DHP. The first basis time course has two kinetic components with time constants of tau(11) approximate to 9 ps and tau(12) approximate to 50 ps that correspond to geminate recombination. The fast geminate process tau(11) arises from a contact pair with the heme iron in a bound state with S) 3/2 spin. The slow geminate process tau(12) corresponds to the recombination from a more remote docking site > 3 angstrom from the heme iron with the greater barrier corresponding to a S) 5/ 2 spin state. The second SVD basis spectrum represents a time- dependent Soret band shift indicative of heme photophysical processes and protein relaxation with time constants of tau(21) approximate to 3 ps and tau(22) approximate to 17 ps, respectively. A comparison between the more rapid rate constant of the slow geminate phase in DHP- NO and horse heart myoglobin ( HHMbNO) or sperm whale myoglobin ( SWMbNO) suggests that protein interactions with photolyzed NO are weaker in DHP than in the wild- type MbNOs, consistent with the hydrophobic distal pocket of DHP. The slower protein relaxation rate tau(22) in DHP- NO relative to HHMbNO implies less effective trapping in the docking site of the distal pocket and is consistent with a greater yield for the fast geminate process. The trends observed for DHP- NO also hold for the H64V mutant of SWMb ( H64V MbNO), consistent with a more hydrophobic distal pocket for that protein as well. We examine the influence of solution viscosity on NO recombination by varying the glycerol content in the range from 0% to 90% ( v/ v). The dominant effect of increasing viscosity is the increase of the rate of the slow geminate process, tau(12), coupled with a population decrease of the slow geminate component. Both phenomena are similar to the effect of viscosity on wild- type Mb due to slowing of protein relaxation resulting from an increased solution viscosity and protein surface dehydration. (10.1021/jp056790m)
  DOI : 10.1021/jp056790m
• Second harmonic generation by collagens I and IV: chiroptical and structural effects
  
  • Pena Ana-Maria
  • Boulesteix Thierry
  • Dartigalongue Thibault
  • Schanne-Klein Marie-Claire
  , 2006.
• Studying intra-protein signaling intermediates in the heme-based oxygen sensor protein FixL using sub-picosecond transient Raman spectroscopy
  
  • Vos Marten H.
  , 2006, pp.oral.
• Dynamique interne dans les hémoprotéines vue par spectroscopie ultrarapide
  
  • Vos Marten H.
  , 2006.
• Coupling between surface plasmons in subwavelength hole arrays
  
  • Masson Jean-Baptiste
  • Gallot Guilhem
  Physical Review B: Condensed Matter and Materials Physics (1998-2015), American Physical Society, 2006, 73, pp.121401.
• Ionic contrast terahertz near field imaging of axonal water fluxes
  
  • Masson Jean-Baptiste
  • Sauviat Martin-Pierre
  • Martin Jean-Louis
  • Gallot Guilhem
  Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2006, 103 (13), pp.4808-4812.
• Manipulation of morphogenetic movements in live Drosophila embryos using femtosecond pulses
  
  • Supatto Willy
  • Débarre Delphine
  • Martin Jean-Louis
  • Schanne-Klein Marie-Claire
  • Farge Emmanuel
  • Beaurepaire Emmanuel
  , 2006.
• La transglutaminase tissulaire promeut l'organisation fibrillaire du collagène et la progression de la fibrose rénale hypertensive dépendante de l'angiotensine II. (sélectionné pour le prix poster)
  
  • Hernest Monica
  • Pena Ana-Maria
  • Beaurepaire Emmanuel
  • Chatziantoniou C.
  • Martin Jean-Louis
  • Schanne-Klein Marie-Claire
  , 2006.
• Optical in situ size determination of single lanthanide-ion doped oxide nanoparticles
  
  • Casanova Didier
  • Giaume Domitile
  • Beaurepaire Emmanuel
  • Gacoin Thierry
  • Boilot Jean-Pierre
  • Alexandrou Antigoni
  Applied Physics Letters, American Institute of Physics, 2006, 89 (25), pp.253103. We show that the size of a lanthanide-ion doped nanoparticle can be accurately determined from its luminosity. The optically determined size distribution is in very good agreement with the distribution obtained from transmission electron microscopy. These data confirm that single nanoparticles are visualized in microscopy experiments. Nanoparticles as small as 13 nm are detectable with integration times of 500 ms. (c) 2006 American Institute of Physics. (10.1063/1.2405871)
  DOI : 10.1063/1.2405871
• True near field versus contrast near field imaging.
  
  • Masson Jean-Baptiste
  • Gallot Guilhem
  Optics Express, Optical Society of America - OSA Publishing, 2006, 14 (24), pp.11566-11574. We demonstrate that in near field imaging, interaction between light and sample can be divided into two main areas: the true near field and the contrast near field domain. We performed extensive numerical simulations in order to identify the limits of these areas, and to investigate contrast near field imaging in which much easier propagation calculation can be achieved. Finally, we show an application with terahertz axonal imaging. © 2006 Optical Society of America (10.1364/OE.14.011566)
  DOI : 10.1364/OE.14.011566
• Ultrafast Conformational Changes in Carboxy-Myoglobin Studied by Time-Resolved Circular Dichroism
  
  • Dartigalongue Thibault
  • Hache François
  , 2006.
• Dynamics of NO rebinding to the heme domain of NO synthase-like proteins from bacterial pathogens
  
  • Gautier Christian
  • Martasek P.
  • Mikula I.
  • Nioche P.
  • Raman C.S.
  • Slama-Schwok Anny
  Nitric Oxide, 2006, 15 (4), pp.312. Some Gram-positive bacterial pathogens harbor a gene that encodes a protein (HNS, Heme domain of NO Synthase-like proteins) with striking sequence identity to the oxygenase domain of mammalian NO synthases (NOS). However, they lack the N-terminal and the Zn-cysteine motif participating to the stability of an active dimer in the mammalian isoforms. The unique properties of HNS make it an excellent model system for probing how the heme environment tunes NO dynamics and for comparing it to the endothelial NO synthase heme domain (eNOSHD) using ultrafast transient spectroscopy. NO rebinding in HNS from Staphylococcus aureus (SA-HNS) is faster than that measured for either Bacillus anthracis (BA-HNS) or for eNOSHD in both oxidized and reduced forms in the presence of arginine. To test whether these distinct rates arise from different energy barriers for NO recombination, we measured rebinding kinetics at several temperatures. Our data are consistent with different barriers for NO recombination in SA-HNS and BA-HNS and the presence of a second NO-binding site. The hypothesis that an additional NO-binding cavity is present in BA-HNS is also consistent with the effect of the NO concentration on its rebinding. The lack of the effect of NO concentration on the geminate rebinding in SA-HNS could be due to an isolated second site. We confirm the existence of a second NO site in the oxygenase domain of the reduced eNOS as previously hypothesized [A. Slama-Schwok, M. Négrerie, V. Berka, J.C. Lambry, A.L. Tsai, M.H. Vos, J.L. Martin, Nitric oxide (NO) traffic in endothelial NO synthase. Evidence for a new NO binding site dependent on tetrahydrobiopterin? J. Biol. Chem. 277 (2002) 7581-7586]. This site requires the presence of arginine and BH4; and we propose that NO dynamic and escape from eNOS is regulated by the active site H-bonding network connecting between the heme, the substrate, and cofactor. Cop. 2006 Elsevier Inc. All rights reserved. (10.1016/j.niox.2006.03.010)
  DOI : 10.1016/j.niox.2006.03.010
• Interferometric Fourier transform coherent anti-stokes Raman scattering
  
  • Cui M.
  • Joffre Manuel
  • Skodack J.
  • Ogilvie Jennifer P.
  Optics Express, Optical Society of America - OSA Publishing, 2006, 14 (18), pp.8448-8458. We present an interferometric time-domain Fourier transform implementation of coherent anti-Stokes Raman scattering (CARS). Based on a single femtosecond laser source, the method provides a straight-forward scheme for obtaining high resolution CARS spectra. We give a theoretical description of the method, and demonstrate good agreement between simulation and experimental CARS spectra. We also discuss the method's relation to other CARS approaches for microscopy and microspectroscopy applications. Cop. 2006 Optical Society of America. (10.1364/OE.14.008448)
  DOI : 10.1364/OE.14.008448
• A Hydrophobic Distal Pocket Affects NO-heme Geminate Recombination Dynamics in Dehaloperoxidase and H64V Myoglobin
  
  • Franzen Stefan
  • Jasaitis Audrius
  • Belyea Jennifer
  • Brewer Scott
  • Casey Romain
  • Macfarlane a W Iv
  • Stanley R.
  • Vos Marten H.
  • Martin Jean-Louis
  Journal of Physical Chemistry B, American Chemical Society, 2006, 110, pp.14483-14493.
• Time-resolved circular dichroism in carbonmonoxy-myoglobin: The central role of the proximal histidine
  
  • Dartigalongue Thibault
  • Hache François
  Chirality, Wiley, 2006, 18 (4), pp.273. A calculation of the circular dichroism (CD) spectra of carbonmonoxy-and deoxy-myoglobin is carried out in relation to a time-resolved CD experiment. This calculation allows us to assign a dominant role to the proximal histidine in the definition of the electronic normal modes and to interpret the transient CD structure observed in a strain of the proximal histidine. This strain builds up in 10 ps and relaxes in 50 ps as the protein evolves towards its deoxy form. Cop. 2006 Wiley-Liss, Inc. (10.1002/chir.20254)
  DOI : 10.1002/chir.20254
• Imaging lipid bodies in cells and tissues using third-harmonic generation microscopy.
  
  • Débarre Delphine
  • Supatto Willy
  • Pena Ana-Maria
  • Fabre Aurelie J
  • Tordjmann Thierry
  • Combettes Laurent
  • Schanne-Klein Marie-Claire
  • Beaurepaire Emmanuel
  Nature Methods, Nature Publishing Group, 2006, 3 (1), pp.47-53. Lipid bodies have an important role in energy storage and lipid regulation. Here we show that lipid bodies are a major source of contrast in third-harmonic generation (THG) microscopy of cells and tissues. In hepatocytes, micrometer-sized lipid bodies produce a THG signal 1-2 orders of magnitude larger than other structures, which allows one to image them with high specificity. THG microscopy with approximately 1,200 nm excitation can be used to follow the distribution of lipid bodies in a variety of unstained samples including insect embryos, plant seeds and intact mammalian tissue (liver, lung). We found that epi-THG imaging is possible in weakly absorbing tissues because bulk scattering redirects a substantial fraction of the forward-generated harmonic light toward the objective. Finally, we show that the combination of THG microscopy with two-photon and second-harmonic imaging provides a new tool for exploring the interactions between lipid bodies, extracellular matrix and fluorescent compounds (vitamin A, NADH and others) in tissues. (10.1038/nmeth813)
  DOI : 10.1038/nmeth813
• Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: Implications for nitric oxide sensors
  
  • Négrerie Michel
  • Kruglik Sergei G.
  • Lambry Jean-Christophe
  • Vos Marten H.
  • Martin Jean-Louis
  • Franzen S.
  Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281, pp.10389. The influence of the heme iron coordination on nitric oxide binding dynamics was investigated for the myoglobin mutant H93G (H93G-Mb) by picosecond absorption and resonance Raman time-resolved spectroscopies. In the H93G-Mb, the glycine replacing the proximal histidine does not interact with the heme iron so that exogenous substituents like imidazole may coordinate to the iron at the proximal position. Nitrosylation of H93G-Mb leads to either 6- or 5-coordinate species depending on the imidazole concentration. At high concentrations, (imidazole)-(NO)-6-coordinate heme is formed, and the photoinduced rebinding kinetics reveal two exponential picosecond phases (~10 and ~100 ps) similar to those of wild type myoglobin. At low concentrations, imidazole is displaced by the trans effect leading to a (NO)-5-coordinate heme, becoming 4-coordinate immediately after photolysis as revealed from the transient Raman spectrum. In this case, NO rebinding kinetics remain bi-exponential with no change in time constant of the fast component whose amplitude increases with respect to the 6-coordinate species. Bi-exponential NO geminate rebinding in 5-coordinate H93G-Mb is in contrast with the single-exponential process reported for nitrosylated soluble guanylate cyclase (Negrerie, M., Bouzhir, L., Martin, J. L., and Liebl, U. (2001) J. Biol. Chem. 276, 46815-46821). Thus, our data show that the iron coordination state or the heme iron out-of-plane motion are not at the origin of the bi-exponential kinetics, which depends upon the protein structure, and that the 4-coordinate state favors the fast phase of NO geminate rebinding. Consequently, the heme coordination state together with the energy barriers provided by the protein structure control the dynamics and affinity for NO-binding enzymes. Cop. 2006 by The American Society for Biochemistry and Molecular Biology, Inc. (10.1074/jbc.M513375200)
  DOI : 10.1074/jbc.M513375200
• SHG microscopy. Quantitative scoring of kidney collagen fibrosis. (prix du meilleur poster)
  
  • Strupler Mathias
  • Hernest Monica
  • Pena Ana-Maria
  • Martin Jean-Louis
  • Beaurepaire Emmanuel
  • Tharaux Pierre-Louis
  • Schanne-Klein Marie-Claire
  , 2006.
• Generation and complete characterization of intense mid-infrared ultrashort pulses
  
  • Ventalon Cathie
  • Fraser James M.
  • Likforman Jean-Pierre
  • Villeneuve D. M.
  • Corkum Paul B.
  • Joffre Manuel
  Journal of the Optical Society of America B, Optical Society of America, 2006, 23, pp.332.
• Sensitivity of cardiac background inward rectifying K+ outward current (IK1) to the alkaloids lepadiformines A, B, and C
  
  • Sauviat Martin-Pierre
  • Vercauteren J.
  • Grimaud N.
  • Jugé M.
  • Nabil M.
  • Petit J.-Y.
  • Biard J.-F.
  Journal of Natural Products, American Chemical Society, 2006, 69 (4), pp.558. Three marine alkaloids, purified from Clavelina moluccensis, were structurally identified as lepadiformines A, B, and C and studied on frog atrial myocytes IK1, using the patch-clamp technique. Lepadiformine A (0.4 to 3.3 μM) blocked IK1 dose-dependently with an apparent dissociation constant (KD) equal to 1.42 μM and a stoichiometry of 0.77. The block is voltage-dependent, suggesting that lepadiformine A occupies a receptor site located at about two-thirds of the membrane depth. The shortening of the aliphatic chain at position C13 of lepadiformine B decreased the potency of the molecule to block IK1 but not the affinity (KD = 1.56 μM) and stoichiometry (0.72). Additional deletion of the oxygenated side chain at C2 in lepadiformine C markedly decreased the inhibitory effect of the molecule. In conclusion, lepadiformine modulates IK1 response in cardiac muscle. The oxygenated side chain in C2 is implicated in the affinity of lepadiformine, which behaved as an amine, for a receptor located near or inside the IK1 pore, and the aliphatic chain length at position C13 is involved in the degree of IK1 blockage. (10.1021/np050215s)
  DOI : 10.1021/np050215s