Low temperature surface-enhanced resonance raman scattering (SERRS) from cytochromes

Therese M. Cotton; Vicki Schlegel; Randall E. Holt; Barbara Swanson; Paul O. de Montellano

doi:10.1117/12.951597

Low temperature surface-enhanced resonance raman scattering (SERRS) from cytochromes

Therese M. Cotton, Vicki Schlegel, Randall E. Holt, Barbara Swanson, Paul O. de Montellano

Food Science and Technology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

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.

Original language	English (US)
Pages (from-to)	263-270
Number of pages	8
Journal	Proceedings of SPIE - The International Society for Optical Engineering
Volume	1055
DOIs	https://doi.org/10.1117/12.951597
State	Published - Jul 5 1989

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Condensed Matter Physics
Computer Science Applications
Applied Mathematics
Electrical and Electronic Engineering

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title = "Low temperature surface-enhanced resonance raman scattering (SERRS) from cytochromes",

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.",

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T1 - Low temperature surface-enhanced resonance raman scattering (SERRS) from cytochromes

AU - Cotton, Therese M.

AU - Schlegel, Vicki

AU - Holt, Randall E.

AU - Swanson, Barbara

AU - de Montellano, Paul O.

PY - 1989/7/5

Y1 - 1989/7/5

N2 - 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.

AB - 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.

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