Time-resolved circular dichroism spectroscopy: experiment, theory, and applications to biological systems

Lewis, James W.; Goldbeck, Robert A.; Kliger, David S.; Xie, X. Sunney; Dunn, Robert C.; Simon, John D.

doi:10.1021/j100192a016

Cited by 81 publications

(61 citation statements)

References 6 publications

(6 reference statements)

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“…Moreover, changes in the optical activity of a lumiphore following electronic excitation (as due to realignment of the excited chromophore relative to its domain) can be followed through the time dependence of the emission anisotropy factor. Techniques based on time-resolved optical activity measurements are demonstrated by recent work in other laboratories for both absorption (13) and emission (14,15) in the millisecond regime of chromophores in chiral environments.…”

Section: Resultsmentioning

confidence: 99%

Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenase.

Schauerte

Schlyer

Steel

et al. 1995

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

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Circularly polarized luminescence (CPL) spectroscopy provides information on the excited-state chirality of a lumiphore analogous but complementary to information regarding the ground-state chirality derived from circular dichroism. While CPL spectra are sensitive to the structure surrounding the lumiphore, their applicability to studies of complex biomolecules is limited by the fact that as a rule these molecules contain several identical lumiphores in different environments (e.g., tryptophan residues in a protein). Moreover, the ensemble of biomolecules in solution frequently exists in an equilibrium among different conformational states that interconvert on a time scale longer than that involved in the emission of luminescence. Hence, a typical CPL spectrum is a superposition of several independent contributions with a high degree of spectral overlap. One effective approach for the resolution of such composite spectra is by monitoring the time evolution of the CPL signal and the luminescence decay after electronic excitation of the lumiphore and correlating the CPL components to those obtained from analysis of the luminescence decay. Individual terms in the CPL may then be assigned distinct decay components. Time-dependent CPL may also arise from excited-state interactions of the lumiphore that affect the local chiral properties during the excited state lifetime. In such cases each lumiphore may possess a timedependent CPL, and the time-resolved CPL (TR-CPL) then can be used to obtain information on the dynamics of excitedstate interactions.We have recently utilized time-resolved optical activity and demonstrated that we could assign each of the four components obtained in the analysis of the decay of the roomtemperature phosphorescence of bacterial glucose-6-phosphate dehydrogenase (G6PDH) with a time-independent gem derived from the analysis of the time-resolved circularly polarized phosphorescence from the enzyme's tryptophan residues (4). This assignment allowed us to conclude that the room-temperature phosphorescence of G6PDH originates in three or four tryptophan residues, each with a unique, timeindependent CPL contribution.In

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Section: Resultsmentioning

confidence: 99%

Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenase.

Schauerte

Schlyer

Steel

et al. 1995

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

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“…Such conditions are disadvantageous for femtosecond spectroscopy, especially if one wants to apply pulse-shaping techniques, where small volumes and short path lengths are needed to achieve high intensities for nonlinear excitations and to avoid pulse distortion upon propagation through the sample. In this paper, we do not probe ultrafast chirality changes, as demonstrated (or proposed) by probing ultrafast changes in optical rotation [1][2][3][4] or circular dichroism [1][2][3][4][5][6][7][8][9][10][11][12], but we rather make use of optical rotation changes due to a stable photo- product as a probe for ultrafast dynamics initiated with femtosecond laser pulses. For an experimental implementation of this concept, we present an accumulative polarimeter setup with short path length that is fast and sensitive enough to overcome the mentioned complications.…”

Section: Introductionmentioning

confidence: 99%

Precise and rapid detection of optical activity for accumulative femtosecond spectroscopy

et al. 2012

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We present polarimetry, i.e. the detection of optical rotation of light polarization, in a configuration suitable for femtosecond spectroscopy. The polarimeter is based on common-path optical heterodyne interferometry and provides fast and highly sensitive detection of rotatory power. Femtosecond pump and polarimeter probe beams are integrated into a recently developed accumulative technique that further enhances sensitivity with respect to single-pulse methods. The high speed of the polarimeter affords optical rotation detection during the pump-pulse illumination period of a few seconds. We illustrate the concept on the photodissociation of the enantiomers of methyl p-tolyl sulfoxide. The sensitivity of rotatory detection, i.e. the minimum rotation angle that can be measured, is determined experimentally including all noise sources to be 0.10 milli-degrees for a measurement time of only one second and an interaction length of 250 µm. The suitability of the presented setup for femtosecond studies is demonstrated in a non-resonant two-photon photodissociation experiment. 3682-3692 (1991). 9. S. Milder, S. Bjorling, I. Kuntz, and D. Kliger, "Time-resolved circular dichroism and absorption studies of the photolysis reaction of (carbonmonoxy)myoglobin," Biophys. J. 53, 659-664 (1988

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“…1 [29]. Conventionally, P is used to represent the special pair, which consists of two bacterial chlorophylls separated by $ 3 Å , and B and H are used to denote the bacteriochlorophyll and bacteriopheophytin, respectively.…”

Section: Introductionmentioning

confidence: 99%

Ultrafast Dynamics and Spectroscopy of Bacterial Photosynthetic Reaction Centers

Lin¹,

Chang²,

Liang³

et al. 2002

Advances in Chemical Physics

115

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Time-resolved circular dichroism spectroscopy: experiment, theory, and applications to biological systems

Cited by 81 publications

References 6 publications

Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenase.

Nanosecond time-resolved circular polarization of fluorescence: study of NADH bound to horse liver alcohol dehydrogenase.

Precise and rapid detection of optical activity for accumulative femtosecond spectroscopy

Ultrafast Dynamics and Spectroscopy of Bacterial Photosynthetic Reaction Centers

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