Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity analysis of Cytochrome C

Christian Johannessen, Salim Abdali, Peter C. White

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

High quality Resonance Raman (RR) and resonance Raman Optical Activity (ROA) spectra of cytochrome c were obtained in order to perform full assignment of spectral features of the resonance ROA spectrum. The resonance ROA spectrum of cytochrome c revealed a distinct spectral signature pattern due to resonance enhanced skeletal porphyrin vibrations, more pronounced than any contribution from the protein back-bone. Combining the intrinsic resonance enhancement of cytochrome c with surface plasmon enhancement by colloidal silver particles, the Surface Enhanced Resonance Raman Scattering (SERRS) and Chiral Enhanced Raman Spectroscopy (ChERS) spectra of the protein were successfully obtained at very low concentration (as low as 1 µM). The assignment of spectral features was based on the information obtained from the RR and resonance ROA spectra. Excellent agreement between RR and SERRS spectra is reported, while some disparities were observed between the resonance ROA and ChERS spectra. The difference can be ascribed perturbations of the physical properties of the protein upon adhesion to the surface of the silver colloids.
Original languageEnglish
JournalJournal of Physical Chemistry
Volume111
Pages (from-to)7771-7776
ISSN0022-3654
DOIs
Publication statusPublished - 2007

Cite this

Johannessen, Christian ; Abdali, Salim ; White, Peter C. / Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity analysis of Cytochrome C. In: Journal of Physical Chemistry. 2007 ; Vol. 111. pp. 7771-7776.
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title = "Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity analysis of Cytochrome C",
abstract = "High quality Resonance Raman (RR) and resonance Raman Optical Activity (ROA) spectra of cytochrome c were obtained in order to perform full assignment of spectral features of the resonance ROA spectrum. The resonance ROA spectrum of cytochrome c revealed a distinct spectral signature pattern due to resonance enhanced skeletal porphyrin vibrations, more pronounced than any contribution from the protein back-bone. Combining the intrinsic resonance enhancement of cytochrome c with surface plasmon enhancement by colloidal silver particles, the Surface Enhanced Resonance Raman Scattering (SERRS) and Chiral Enhanced Raman Spectroscopy (ChERS) spectra of the protein were successfully obtained at very low concentration (as low as 1 µM). The assignment of spectral features was based on the information obtained from the RR and resonance ROA spectra. Excellent agreement between RR and SERRS spectra is reported, while some disparities were observed between the resonance ROA and ChERS spectra. The difference can be ascribed perturbations of the physical properties of the protein upon adhesion to the surface of the silver colloids.",
author = "Christian Johannessen and Salim Abdali and White, {Peter C.}",
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Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity analysis of Cytochrome C. / Johannessen, Christian; Abdali, Salim; White, Peter C.

In: Journal of Physical Chemistry, Vol. 111, 2007, p. 7771-7776.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Resonance Raman Optical Activity and Surface Enhanced Resonance Raman Optical Activity analysis of Cytochrome C

AU - Johannessen, Christian

AU - Abdali, Salim

AU - White, Peter C.

PY - 2007

Y1 - 2007

N2 - High quality Resonance Raman (RR) and resonance Raman Optical Activity (ROA) spectra of cytochrome c were obtained in order to perform full assignment of spectral features of the resonance ROA spectrum. The resonance ROA spectrum of cytochrome c revealed a distinct spectral signature pattern due to resonance enhanced skeletal porphyrin vibrations, more pronounced than any contribution from the protein back-bone. Combining the intrinsic resonance enhancement of cytochrome c with surface plasmon enhancement by colloidal silver particles, the Surface Enhanced Resonance Raman Scattering (SERRS) and Chiral Enhanced Raman Spectroscopy (ChERS) spectra of the protein were successfully obtained at very low concentration (as low as 1 µM). The assignment of spectral features was based on the information obtained from the RR and resonance ROA spectra. Excellent agreement between RR and SERRS spectra is reported, while some disparities were observed between the resonance ROA and ChERS spectra. The difference can be ascribed perturbations of the physical properties of the protein upon adhesion to the surface of the silver colloids.

AB - High quality Resonance Raman (RR) and resonance Raman Optical Activity (ROA) spectra of cytochrome c were obtained in order to perform full assignment of spectral features of the resonance ROA spectrum. The resonance ROA spectrum of cytochrome c revealed a distinct spectral signature pattern due to resonance enhanced skeletal porphyrin vibrations, more pronounced than any contribution from the protein back-bone. Combining the intrinsic resonance enhancement of cytochrome c with surface plasmon enhancement by colloidal silver particles, the Surface Enhanced Resonance Raman Scattering (SERRS) and Chiral Enhanced Raman Spectroscopy (ChERS) spectra of the protein were successfully obtained at very low concentration (as low as 1 µM). The assignment of spectral features was based on the information obtained from the RR and resonance ROA spectra. Excellent agreement between RR and SERRS spectra is reported, while some disparities were observed between the resonance ROA and ChERS spectra. The difference can be ascribed perturbations of the physical properties of the protein upon adhesion to the surface of the silver colloids.

U2 - 10.1021/jp0705267

DO - 10.1021/jp0705267

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VL - 111

SP - 7771

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JO - Journal of Physical Chemistry

JF - Journal of Physical Chemistry

SN - 0022-3654

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