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    Fourier Transform Raman Spectroscopy of Photoactive Proteins with Near-Infrared Excitation

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    JohnsonC_AS_44(7)1103.pdf (354.3Kb)
    Issue Date
    1990-07-01
    Author
    Johnson, Carey K.
    Rubinovitz, Ronald
    Publisher
    Optical Society of America
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
    Published Version
    http://www.opticsinfobase.org/as/abstract.cfm?URI=as-44-7-1103
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    Abstract
    The Fourier transform (FT) Raman spectroscopic treatment of the photoactive proteins bacteriorhodopsin and the photosynthetic reaction center is reported, with excitation at 1.06 μm. Excitation at this wavelength circumvents the limitations on resonance Raman spectroscopy of these proteins imposed by their photolability and by the fluorescence of free pigments or impurities. The spectra are dominated by nonresonant Raman scattering by the protein-bound pigments retinal (in bacteriorhodopsin) and bacteriopheophytin, bacteriochlorophyll, and carotenoids (in reaction centers). The relative intensities of retinylidene modes in the spectrum for nonresonant FT Raman spectroscopy of bacteriorhodopsin are nearly identical to those observed in the resonance Raman spectrum of bacteriorhodopsin.
    Description
    This is the publisher's version, also available electronically from http://www.opticsinfobase.org/as/abstract.cfm?URI=as-44-7-1103.
    URI
    http://hdl.handle.net/1808/16119
    ISSN
    0003-7028
    Collections
    • Chemistry Scholarly Works [610]
    Citation
    Johnson, Carey K.; Rubinovitz, Ronald. (1990). "Fourier Transform Raman Spectroscopy of Photoactive Proteins with Near-Infrared Excitation." Journal of Applied Spectroscopy, 44(7):1103-1106. http://www.opticsinfobase.org/as/abstract.cfm?URI=as-44-7-1103

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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