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Fourier-transform Raman spectroscopy applied to photobiological systems

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Siebert,  Friedrich
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;
lnstitut für Biophysik und Strahlenbiologie der Albert-Ludwig-Universität Freiburg, 7800 Freiburg im Breisgau, Federal Republic of Germany;

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Citation

Sawatzki, J., Fischer, R., Scheer, H., & Siebert, F. (1990). Fourier-transform Raman spectroscopy applied to photobiological systems. Proceedings of the National Academy of Sciences of the United States of America, 87(15), 5903-5906. doi:10.1073/pnas.87.15.5903.


Cite as: https://hdl.handle.net/21.11116/0000-0007-AEE7-1
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.