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Proceedings Paper

Low Temperature Surface-Enhanced Resonance Raman Scattering (SERRS) From Cytochromes
Author(s): Therese M. Cotton; Vicki Schlegel; Randall E. Holt; Barbara Swanson; Paul Ortiz de Montellano
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Paper Abstract

Surface-enhanced resonance Raman scattering (SERRS) studies of cytochrome c (cyt c) and cytochrome P450 (cyt P450) as a function of laser irradiation time have demonstrated that the proteins are extremely sensitive to photodegradation. The results suggest that previous SERRS reports of hemoprotein denaturation on Ag surfaces may reflect photosensitivity rather than an effect of the protein-surface interaction. Photodamage was eliminated by submersion of the electrode into liquid nitrogen. This procedure resulted in stable SERRS spectra, even with prolonged irradiation. The use of a diode array detector also substantially reduces the laser exposure period ( < 1 minute) required to observe SERRS spectra of the protein. The application of low temperature SERRS spectroscopy to the study of substrate binding in P450b provided evidence for spin state conversion in the presence of substrate.

Paper Details

Date Published: 5 July 1989
PDF: 8 pages
Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); doi: 10.1117/12.951597
Show Author Affiliations
Therese M. Cotton, University of Nebraska-Lincoln (United States)
Vicki Schlegel, University of Nebraska-Lincoln (United States)
Randall E. Holt, University of Nebraska-Lincoln (United States)
Barbara Swanson, University of California (United States)
Paul Ortiz de Montellano, University of California (United States)


Published in SPIE Proceedings Vol. 1055:
Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology
Fran Adar; James E. Griffiths; Jeremy M. Lerner, Editor(s)

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