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Fourier-transform Raman Spectroscopy Applied to Photobiological Systems

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Specialty Science
Date 1990 Aug 1
PMID 11607094
Citations 8
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Abstract

Fluorescence and initiation of photoreactions are problems frequently encountered with resonance Raman spectroscopy of photobiological systems. These problems can be circumvented with Fourier-transform Raman spectroscopy by using the 1064-nm wavelength of a continuous wave neodymium-yttrium/aluminum-garnet laser as the probing beam. This wavelength is far from the absorption band of most pigments. Yet, the spectra of the investigated systems--bacteriorhodopsin, rhodopsin, and phycocyanin--show that these systems are still dominated by the chromophore, or that preresonant Raman scattering is still prevalent. Only for rhodopsin were contributions of the protein and the membrane discernible. The spectra of phycocyanin differ considerably from those obtained by excitation into the UV-absorption band. The results show the usefulness of this method and its wide applicability. In addition, analysis of the relative preresonant scattering cross sections may provide a detailed insight into the scattering mechanism.

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References
1.
Gerwert K, Siebert F . Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals. EMBO J. 1986; 5(4):805-11. PMC: 1166862. DOI: 10.1002/j.1460-2075.1986.tb04285.x. View

2.
Loppnow G, Mathies R . Excited-state structure and isomerization dynamics of the retinal chromophore in rhodopsin from resonance Raman intensities. Biophys J. 1988; 54(1):35-43. PMC: 1330313. DOI: 10.1016/S0006-3495(88)82928-X. View

3.
Angel I, Taranger M . Coupling between hypothalamic alpha 2-adrenoceptors and [3H]mazindol binding site in response to several hyperglycaemic stimuli in mice. Brain Res. 1989; 490(2):367-72. DOI: 10.1016/0006-8993(89)90256-4. View

4.
Ekholm S, Simon J . Magnetic resonance imaging and the acquired immunodeficiency syndrome dementia complex. Acta Radiol. 1988; 29(2):227-30. View

5.
Schirmer T, Bode W, Huber R . Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1 and 2.5 A resolution. A common principle of phycobilin-protein interaction. J Mol Biol. 1987; 196(3):677-95. DOI: 10.1016/0022-2836(87)90040-4. View