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5 July 1989 Low Temperature Surface-Enhanced Resonance Raman Scattering (SERRS) From Cytochromes
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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.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Therese M. Cotton, Vicki Schlegel, Randall E. Holt, Barbara Swanson, and Paul Ortiz de Montellano "Low Temperature Surface-Enhanced Resonance Raman Scattering (SERRS) From Cytochromes", Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989);

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