Characterization of stimulated Raman scattering of hydrogen and methane gases as a light source for picosecond time-resolved Raman spectroscopy

Uesugi, Yoshihiko; Mizutani, Yasuhisa; Kruglik, Sergei G.; Shvedko, A. G.; Orlovich, V. A.; Kitagawa, Teizo

doi:10.1002/(sici)1097-4555(200004)31:4<339::aid-jrs547>3.0.co;2-a

Cited by 24 publications

(2 citation statements)

References 30 publications

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“…43 repetition rate are a few of the workhorses used as pump source in nanosecond TR3 experiments. A number of wavelengths can be produced for pump and probe by using the harmonics of Nd:YAG for pumping dye lasers, 49,50 optical parametric oscillators (OPO), 51 and gas- 52 and solid-state Raman shifters. 53 The output wavelengths from these sources can further be manipulated (doubling, tripling, mixing) to produce various continuously tunable discrete colors of monochromatic light spanning from the DUV to the NIR region.…”

Section: Fig 3 Schematic Illustration Of the Four Possible Cases Inmentioning

confidence: 99%

Time-Resolved Resonance Raman Spectroscopy: Exploring Reactive Intermediates

2011

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The study of reaction mechanisms involves systematic investigations of the correlation between structure, reactivity, and time. The challenge is to be able to observe the chemical changes undergone by reactants as they change into products via one or several intermediates such as electronic excited states (singlet and triplet), radicals, radical ions, carbocations, carbanions, carbenes, nitrenes, nitrinium ions, etc. The vast array of intermediates and timescales means there is no single "do-it-all" technique. The simultaneous advances in contemporary time-resolved Raman spectroscopic techniques and computational methods have done much towards visualizing molecular fingerprint snapshots of the reactive intermediates in the microsecond to femtosecond time domain. Raman spectroscopy and its sensitive counterpart resonance Raman spectroscopy have been well proven as means for determining molecular structure, chemical bonding, reactivity, and dynamics of short-lived intermediates in solution phase and are advantageous in comparison to commonly used time-resolved absorption and emission spectroscopy. Today time-resolved Raman spectroscopy is a mature technique; its development owes much to the advent of pulsed tunable lasers, highly efficient spectrometers, and high speed, highly sensitive multichannel detectors able to collect a complete spectrum. This review article will provide a brief chronological development of the experimental setup and demonstrate how experimentalists have conquered numerous challenges to obtain background-free (removing fluorescence), intense, and highly spectrally resolved Raman spectra in the nanosecond to microsecond (ns-μs) and picosecond (ps) time domains and, perhaps surprisingly, laid the foundations for new techniques such as spatially offset Raman spectroscopy.

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Section: Fig 3 Schematic Illustration Of the Four Possible Cases Inmentioning

confidence: 99%

Time-Resolved Resonance Raman Spectroscopy: Exploring Reactive Intermediates

2011

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“…In the last decade, a large number of TR 3 studies [18,19,31 -33] were performed with a system based on picosecond Ti : sapphire laser [38] having a temporal resolution of about 2 ps. The tunability of the pump and probe pulses was generally achieved by means of a water continuum generation, [38] by a Raman shifter, [39,40] or by optical parametric generation/amplification (OPG/OPA). [38,41] A Kerr-gated TR 3 spectrometer with about 1 ps resolution based on OPG/OPA has been reported, [41 -43] which allowed wide tuning of both pump and probe pulses by frequency mixing.…”

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confidence: 99%

Sub‐picosecond Raman spectrometer for time‐resolved studies of structural dynamics in heme proteins

Kruglik

Lambry

Martin

et al. 2011

J Raman Spectroscopy

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International audienceWe describe a pump-probe Raman spectrometer based on a femtosecond Ti:sapphire laser, an optical parametric generator and two optical parametric amplifiers for time-resolved studies, with emphasis on the structural dynamics in heme proteins. The system provides a 100-fs pump pulse tunable in the range 500-600 nm and a transform-limited sub-picosecond probe pulse tunable in the range 390-450 nm. The spectrometer has spectral (25 cm(-1)) and temporal (similar to 0.7 ps) resolutions which constitute an effective compromise for identifying transient heme protein species and for following their structural evolution by spontaneous Raman scattering in the time range 0.5 ps to 2 ns. This apparatus was applied to time-resolved studies of a broad range of heme proteins, monitoring the primary dynamics of photoinduced heme coordination state and structural changes, its interaction with protein side-chains and diatomic gaseous ligands, as well as heme vibrational cooling. The treatment of transient Raman spectra is described in detail, and the advantages and shortcomings of spontaneous resonance Raman spectroscopy for ultrafast heme proteins studies are discussed. We demonstrate the efficiency of the constructed spectrometer by measuring Raman spectra in the sub-picosecond and picosecond time ranges for the oxygen-storage heme protein myoglobin and for the oxygen-sensor heme protein FixLH in interaction with the diatomic gaseous ligands CO, NO, and O-2. Copyright (C) 2010 John Wiley and Sons, Ltd

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Time‐resolved resonance Raman study on ultrafast structural relaxation and vibrational cooling of photodissociated carbonmonoxy myoglobin

2002

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A localized small structural change is converted to a higher order conformational change of protein and extends to a mesoscopic scale to induce a physiological function. To understand such features of protein, ultrafast dynamics of myoglobin (Mb) following photolysis of carbon monoxide were investigated. Recent results are summarized here with a stress on structural and vibrational energy relaxation. The core expansion of heme takes place within 2 ps but the out of plane displacement of the heme iron and the accompanying protein conformational change occur in 10 and 100 s of the picosecond regimes, respectively. Unexpectedly, it was found from UV resonance Raman spectra that Trp7 in the N-terminal region and Tyr151 in the C-terminal region undergo appreciable structural changes upon ligand binding-dissociation while Tyr104, Tyr146, and Trp14 do not. Because of the communication between the movements of these surface residues and the heme iron, the rate of spectral change of the iron-histidine (Fe- His) stretching band after CO photodissociation is influenced by the viscosity of solvent. Temporal changes of the anti-Stokes Raman intensity demonstrated immediate generation of vibrationally excited heme upon photodissociation and its decay with a time constant of 1-2 ps.

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Characterization of stimulated Raman scattering of hydrogen and methane gases as a light source for picosecond time-resolved Raman spectroscopy

Cited by 24 publications

References 30 publications

Time-Resolved Resonance Raman Spectroscopy: Exploring Reactive Intermediates

Time-Resolved Resonance Raman Spectroscopy: Exploring Reactive Intermediates

Sub‐picosecond Raman spectrometer for time‐resolved studies of structural dynamics in heme proteins

Time‐resolved resonance Raman study on ultrafast structural relaxation and vibrational cooling of photodissociated carbonmonoxy myoglobin

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