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  Fourier-transform Raman spectroscopy applied to photobiological systems

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.

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 Creators:
Sawatzki, Jürgen1, Author
Fischer, Richard2, Author
Scheer, Hugo2, Author
Siebert, Friedrich3, 4, Author           
Affiliations:
1Bruker Analytische Messtechnik GmbH, Karlsruhe, Federal Republic of Germany, ou_persistent22              
2Botanisches Institut der Universität München, 8000 München, Federal Republic of Germany, ou_persistent22              
3Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society, ou_3273415              
4lnstitut für Biophysik und Strahlenbiologie der Albert-Ludwig-Universität Freiburg, 7800 Freiburg im Breisgau, Federal Republic of Germany, ou_persistent22              

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Free keywords: resonance Raman spectroscopy; preresonant Raman scattering; Raman scattering cross section
 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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Language(s): eng - English
 Dates: 1990-05-031990-08-01
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.87.15.5903
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 87 (15) Sequence Number: - Start / End Page: 5903 - 5906 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230