Ultrashort intramolecular and intermolecular vibrational energy transfer of polyatomic molecules in liquids

Seilmeier, A.; Kaiser, W.

doi:10.1007/bfb0070984

Cited by 29 publications

(39 citation statements)

References 72 publications

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“…Although there is considerable information on these relaxation times (2,45,46), this is not the case for molecules in protein environments or for small molecules or ions in liquids (46). Some molecular vibrations relax by transferring the energy excess directly to the environment, whereas others first undergo intramolecular vibrational-energy redistribution, which can be less sensitive to the environment.…”

Section: Discussionmentioning

confidence: 99%

Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes

Lim

Hamm²,

Hochstrasser³

1998

Proc. Natl. Acad. Sci. U.S.A.

144

181

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The correlation functions of the fluctuations of vibrational frequencies of azide ions and carbon monoxide in proteins are determined directly from stimulated photon echoes generated with femtosecond infrared pulses. The asymmetric stretching vibration of azide bound to carbonic anhydrase II exhibits a pronounced evolution of its vibrational frequency distribution on the time scale of a few picoseconds, which is attributed to modifications of the ligand structure through interactions with the nearby Thr-199. When azide is bound in hemoglobin, a more complex evolution of the protein structure is required to interchange the different ligand configurations, as evidenced by the much slower relaxation of the frequency distribution in this case. The time evolution of the distribution of frequencies of carbon monoxide bound in hemoglobin occurs on the Ϸ10-ps time scale and is very nonexponential. The correlation functions of the frequency fluctuations determine the evolution of the protein structure local to the probe and the extent to which the probe can navigate those parts of the energy landscape where the structural configurations are able to modify the local potential energy function of the probe.Chemical reactions in biology can be controlled by the fluctuations in the energies of the reactant states. When the reactions involve charge translocations, the motions of the charges in the surrounding medium cause changes in the electric fields in the neighborhood of the reacting species, which in turn cause fluctuations of the reactant energies. These fluctuations occur on the time scale of the nuclear motions of the medium. For chemical processes occurring in a protein environment, such as in enzyme catalysis, the dynamics of the protein nuclei can control the reaction. Therefore, it is very important to determine experimentally the essential properties of the fluctuations associated with various observables, such as their mean values, time-correlation functions, and structural origins.The experimental approaches to determining time-correlation functions include spectroscopic line shape measurements and time-domain responses. In the vibrational frequency regime the line-shape approach is a common one (1), although it does not always expose the underlying physical origins of the fluctuations. Time-domain techniques were also developed some time ago that enabled investigations of the various contributions to the line width such as pure dephasing and population relaxation (2). The dephasing times of vibrational transitions having static inhomogeneous distributions can be measured by means of two-pulse photon echoes (3-5). Silvestri et al. (6) have shown that for optical transitions, a photon echo with three pulses can also yield the dynamics of the inhomogeneous distribution. There were many applications of this nonlinear technique in the electronic spectroscopy of dye molecules (refs. 6-8, and see ref. 9 for a review) and of cofactors in biological systems [light-harvesting complex II (10), reaction center (11...

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Section: Discussionmentioning

confidence: 99%

Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes

Lim

Hamm²,

Hochstrasser³

1998

Proc. Natl. Acad. Sci. U.S.A.

144

181

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“…Energy transfer, both intramolecular [47,48] and intermolecular [47,49,50], is another factor that can affect VSFG spectra in a manner that is often not taken into account in traditional models of this spectroscopic technique. For instance, energy transfer can play an important role in the dephasing of vibrational coherences in a manner that has the potential to be orientation-specific at interfaces.…”

Section: Energy Transfermentioning

confidence: 99%

Reexamining the interpretation of vibrational sum-frequency generation spectra

Rivera

Fourkas

2011

International Reviews in Physical Chemistry

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Vibrational sum-frequency generation (VSFG) has become a widely used technique for studying molecular orientation and intermolecular structure at interfaces. Due to the interfacial and vibrational selectivity of this technique, it can be used to probe molecular monolayers that are buried within bulk materials. Here, we present a critical review and examination of the assumptions that are generally used in the interpretation of VSFG spectra. This review focuses on three different aspects of VSFG spectroscopy. First, we examine the effect of dynamics (both reorientation and energy transfer) on the interpretation of VSFG spectra. Second, we consider whether (and under what circumstances) VSFG spectra cannot be interpreted solely in terms of the spectral properties of individual molecules. Third, we consider whether VSFG spectra obtained in different modes (frequency-domain, time-domain and broadband) should provide identical information. We conclude with a discussion of the challenges and opportunities provided by the revised viewpoint of VSFG that we present.

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“…8,24 Pump-probe experiments directly observe energy flow within and out of a molecule by exciting a nonstationary vibrational state with one laser pulse and then probing the evolution of the system as a function of time with a second pulse. 25,26 Infrared absorption, [27][28][29][30][31][32] anti-Stokes Raman scattering, [33][34][35][36][37] and ultraviolet absorption [38][39][40][41][42][43][44][45][46][47][48][49] are the most common methods for probing the vibrational dynamics in the ground electronic state and are generally most useful in the condensed phase where it is possible to obtain a high density of vibrationally excited molecules. In fact, there are relatively few timeresolved studies of IVR in the ground electronic state for gas phase systems.…”

Section: Introductionmentioning

confidence: 99%

Vibrational relaxation of CH3I in the gas phase and in solution

Elles

Cox

Crim

2004

The Journal of Chemical Physics

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Transient electronic absorption measurements reveal the vibrational relaxation dynamics of CH 3 I following excitation of the C-H stretch overtone in the gas phase and in liquid solutions. The isolated molecule relaxes through two stages of intramolecular vibrational relaxation ͑IVR͒, a fast component that occurs in a few picoseconds and a slow component that takes place in about 400 ps. In contrast, a single 5-7 ps component of IVR precedes intermolecular energy transfer ͑IET͒ to the solvent, which dissipates energy from the molecule in 50 ps, 44 ps, and 16 ps for 1 M solutions of CH 3 I in CCl 4 , CDCl 3 , and (CD 3 ) 2 CO, respectively. The vibrational state structure suggests a model for the relaxation dynamics in which a fast component of IVR populates the states that are most strongly coupled to the initially excited C-H stretch overtone, regardless of the environment, and the remaining, weakly coupled states result in a secondary relaxation only in the absence of IET.

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Ultrashort intramolecular and intermolecular vibrational energy transfer of polyatomic molecules in liquids

Cited by 29 publications

References 72 publications

Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes

Protein fluctuations are sensed by stimulated infrared echoes of the vibrations of carbon monoxide and azide probes

Reexamining the interpretation of vibrational sum-frequency generation spectra

Vibrational relaxation of CH3I in the gas phase and in solution

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