A critical test of vibrational dephasing theories in solids using spontaneous Raman scattering in isotopically mixed crystals

Marks, Samuel D.; Cornelius, P. A.; Harris, Charles B.

doi:10.1063/1.440565

Cited by 99 publications

(25 citation statements)

References 42 publications

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“…3) clearly show a nearly symmetric Fe-His mode at all temperatures below freezing and a large (13 cm ') shift in its peak frequency as a function of temperature. Another possible temperature-activated broadening mechanism is vibrational dephasing resulting from anharmonically coupled modes (23)(24)(25). This process predicts a temperaturedependent linewidth and center frequency that are consistent with our observed data.…”

Section: Discussionsupporting

confidence: 81%

“…The predictions of this dephasing model (24,25) are consistent with our data on the Fe-His stretching mode. Within experimental error both the frequency and the linewidth have the same temperature dependence.…”

Section: Discussionsupporting

confidence: 80%

“…For a simple four-level system the temperature dependence of the observed Raman frequency, W. and linewidth, F, may be given by (24,25) Cwo W= AEi/&T Here wo is the uncoupled (low temperature limit) Raman frequency ofwidth Fo andE, is the quantum energy ofthe coupling mode. A and B are constants that contain the anharmonic coupling frequency shift (8w) and the lifetime ofthe coupling mode (T).…”

Section: Discussionmentioning

confidence: 99%

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Resonance Raman detection of structural dynamics at the active site in hemoglobin.

Ondrias¹,

Rousseau²,

Simon³

1982

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

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The iron-histidine stretching mode in deoxyhemoglobin displays a large change in frequency and width upon lowering the temperature from 300 to 10 K. The temperature dependence ofthe data indicates the presence of dynamic processes. The dynamics of this mode in frozen hemoglobins can be qualitatively and quantitatively described as a vibrational dephasing via anharmonic coupling to other vibrations of the heme-imidazole system. The effects that occur at the melting transition in the low frequency modes cannot be quantitatively addressed at this point but may be indicative of the introduction of additional degrees of freedom predicated on protein influences that reflect differences in protein quaternary structure.Large amplitude motions of atoms and groups of atoms have recently been detected in proteins by crystallographic (1, 2) and spectroscopic (3-5) techniques. Although in some instances the functional importance of these motions has not yet been assessed, in others the importance is clear. For example, the heme binding sites in hemoglobin and myoglobin are only accessible because molecular motions occur that modulate the size of the narrow entry channel and thus allow the penetration of small ligands (6). These motions involve both transitions between local minima in the potential energy surface (conformational substates) and thermal population of excited levels. A picture emerges of fluid-like proteins in which molecular groups rotate about single bonds, hydrogen bonds break and reform, and new Van der Waals interactions occur continuously.There have been few reports in which dynamic processes in biomolecules have been probed by Raman scattering (7-10) although its potential for such studies is widely recognized because the Raman frequencies associated with bonds that connect molecular groupings are sensitive to structural dynamics. Resonance Raman scattering studies of dynamic processes in heme proteins are especially promising. The technique can be a sensititive probe of the properties of the active sites where the existence of structural dynamics could have direct functional importance.We report here a resonance Raman investigation of hemoglobin in which we have detected a temperature-dependent variation in the width and position of the mode assigned as the iron-histidine (Fe-His) stretching motion. We interpret these results as evidence for structural dynamics involving fluctuations in the Fe-His bond energy due to anharmonic coupling between modes.METHODS AND MATERIALS Raman scattering data from solutions above and just below freezing were obtained with previously described Raman difference instrumentation (11). Samples were placed in glass or fused silica rotating cells and the scattered light was gathered with 900 collecting optics. For the low temperature studies (< -500C), the rotating liquid cell was removed and liquid samples were placed on the cold finger of a Heli-Tran Cryostat (Air Products and Chemicals, Allentown, PA) where they were frozen either by direct insertion into liquid nit...

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Section: Discussionsupporting

confidence: 81%

Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Resonance Raman detection of structural dynamics at the active site in hemoglobin.

Ondrias¹,

Rousseau²,

Simon³

1982

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

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“…A model for vibrational dephasing by inter-or intramolecular vibrational energy exchange has been developed by Harris and co-workers (Harris et al, 1977(Harris et al, , 1978Shelby et al, 1979;Marks et al, 1980) and . 2 6 , N O .…”

Section: (Z) Heme Photophysicsmentioning

confidence: 98%

Time-resolved Raman spectroscopy with subpicosecond resolution: vibrational cooling and delocalization of strain energy in photodissociated (carbonmonoxy)hemoglobin

Petrich¹,

Martin²,

Houde³

et al. 1987

Biochemistry

115

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A Raman spectrometer that provides both subpicosecond resolution and independent, tunable pump and probe pulses is described. The spectrometer is employed to obtain time-resolved spectra of (carbonmonoxy)hemoglobin (HbCO) at times from 0.2 to 95 ps subsequent to ligand photodissociation. The spectra are interpreted in terms of a vibrationally hot heme that cools substantially in 10 ps. Concomitant with the proposed vibrational cooling is a slower relaxation, which we suggest results from a protein response to heme doming induced by ligand detachment. Results and interpretations are discussed in the context of current models of the heme photophysics and of hemoglobin reactivity.

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“…Contribution of different interactions into shape of a vibrational band was studied in a number of publications [1,4,5,11,12,22,24,29,34]. First, resonant transfer of vibrational energy between identical molecules causes exciton-like broadening of the band.…”

Section: Introductionmentioning

confidence: 99%

Shape of the carbon monoxide infrared absorption band of carboxyheme proteins as a probe of the protein anharmonicity

Stavrov

2010

Spectroscopy

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Abstract. Theory of the CO infrared absorption band of carbonmonoxyheme proteins is developed using results of the theory of optical absorption bandshape of impurity center in crystal. It is shown that the bandshape is controlled by electrostatic interaction to the polar or/and charged heme surrounding. Analysis of the CO bands of different heme proteins brings us to conclusion, that the CO band is broadened by very slow (τ > 10 ps) motions of the heme surrounding and this motion most probably corresponds to the slow collective motion of the protein molecule. Therefore the second moment of the band must depend linearly on temperature at T > 25 K if the heme surrounding moves harmonically. The motion of the protein formed surrounding of the heme is arrested by the glassy protein environment. It is shown that Gaussian is the only possible symmetric shape of the CO band, if the heme surrounding moves harmonically. Deviation from this bandshape is a manifestation of anharmonic character of the surrounding motion. In general, CO infrared absorption band is shown to be an excellent probe of the dynamics of the heme surrounding.

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A critical test of vibrational dephasing theories in solids using spontaneous Raman scattering in isotopically mixed crystals

Cited by 99 publications

References 42 publications

Resonance Raman detection of structural dynamics at the active site in hemoglobin.

Resonance Raman detection of structural dynamics at the active site in hemoglobin.

Time-resolved Raman spectroscopy with subpicosecond resolution: vibrational cooling and delocalization of strain energy in photodissociated (carbonmonoxy)hemoglobin

Shape of the carbon monoxide infrared absorption band of carboxyheme proteins as a probe of the protein anharmonicity

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