Raman Spectroscopy

Campion, Alan

doi:10.1007/978-1-4684-8759-6_8

Cited by 22 publications

(14 citation statements)

References 76 publications

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“…In A , the heme group is located very close to the Ag surface, while in B , the heme group is close to the Au surface and far from the Ag. Since the SERS effect drops off exponentially with distance from the Ag substrate, , much less signal is expected for the geometry shown in B than A . Indeed, the closest heme−Ag distance in B is nearly the same as for the “buried” heme groups unobservable in SERS studies of the multiheme protein, cytochrome c 3 .…”

Section: Resultsmentioning

confidence: 98%

“…This inability to observe SERS signals from even resonantly enhanced chromophores within proteins has been attributed to the distance between the cofactors and the metal surface. The electromagnetic field responsible for much of the enhancement seen in SERS drops off exponentially with distance from the surface. , Thus, the best enhancements are expected (and observed) for groups closest to the roughened metal substrate.…”

Section: Introductionmentioning

confidence: 96%

“…This manuscript reports the preparation, characterization, and use of complexes (conjugates) between cytochrome c (Cc) and colloidal Au nanoparticles as analytes for surface-enhanced Raman scattering (SERS) . The adsorption and conformation of proteins at metal surfaces is critical to many bioanalytical techniques involving transduction of protein-based signals for detection, including electrochemistry, SERS, surface plasmon resonance, and quartz crystal microgravimetry . Unfortunately, adsorption often leads to conformational changes, denaturation, or undesirable protein orientations with respect to the metal substrate .…”

Section: Introductionmentioning

confidence: 99%

“…(i) Much smaller amounts of material are needed for SERS than for RR, because of the large increase in scattering, and because SERS interrogates principally the first molecular layer adsorbed to the enhancing substrate. (ii) The metal surfaces used in SERS are effective quenchers of fluorescence, , a substantial problem in RR experiments . (iii) Since the SERS effect does not require resonant excitation of analyte chromophores, in principle any molecule can be studied by this technique.…”

Section: Introductionmentioning

confidence: 99%

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Protein:Colloid Conjugates for Surface Enhanced Raman Scattering: Stability and Control of Protein Orientation

1998

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Conjugates between cytochrome c (Cc) and colloidal Au particles have been prepared. These conjugates, purified by centrifugation/resuspension, provide a reproducible means of positioning a biomolecule analyte between two metal surfaces: the metal nanoparticle to which the biomolecule is bound and an aggregated Ag sol used as a substrate for surface enhanced Raman scattering (SERS). SERS spectra for Ag:Cc:Au sandwiches made by addition of Cc:Au conjugates to aggregated Ag show that the protein retains its native conformation. Conjugation of Cc to colloidal metal nanoparticles prior to exposure to the SERS substrate can be used as a means of controlling protein orientation with respect to the substrate. In addition, Cc molecules bound to 12-nm diameter Au nanoparticles prior to adsorption to aggregated Ag are more stable to changes in the orientation of the heme with respect to the surface and to surface-induced heme spin state conversion than adsorbed, free Cc. These experiments show that protein:Au conjugates offer benefits as reagents for protein SERS.

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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Protein:Colloid Conjugates for Surface Enhanced Raman Scattering: Stability and Control of Protein Orientation

1998

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“…A rugosidade superficial é uma das condições necessárias para que a superficie sej SERS-ativa. As contribuições podem ser de rugosidade submicroscópica (estruturas com dimensões de 10-100 nm) ou rugosidade em escala atômica (degraus, adatoms ou vacâncias) [26].…”

Section: A Efeito Sers -Surface Enhanced Raman Scaiteringunclassified

A contribuição do mecanismo de transferência de carga para o efeito SERS em interfaces eletroquímicas

Cório¹

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R aman Spectroelectrochemistry

Pemberton¹

2001

Handbook of Vibrational Spectroscopy

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The sections in this article are Introduction Brief Overview of R aman Spectroelectrochemical Approaches Resonance R aman Spectroscopy of Electrochemically Generated Solution Species SERS Surface‐Enhanced Resonance R aman Scattering SERS through Thin Film Transition Metal Electrodes on Enhancing Substrates Surface Plasmon Polariton Enhanced R aman Spectroscopy R aman Spectroelectrochemical Emersion Confocal R aman Spectroelectrochemistry Surface R aman Spectroelectrochemistry without Enhancement Experimental Considerations R aman Spectroelectrochemical Cells Electrode Surfaces and their Preparation R aman Systems for Spectroelectrochemistry Example Applications of R aman Spectroelectrochemistry Characterization of Adsorbed Organics on Electrode Surfaces: 1‐Methylimidazole on Ag Characterization of Specifically Adsorbed Ions at Electrode Surfaces Characterization of Interfacial Solvent Structure at Electrode Surfaces Characterization of Electrochemical Interfaces Using R aman Spectroelectrochemical Emersion

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Raman Spectroscopy

Cited by 22 publications

References 76 publications

Protein:Colloid Conjugates for Surface Enhanced Raman Scattering: Stability and Control of Protein Orientation

Protein:Colloid Conjugates for Surface Enhanced Raman Scattering: Stability and Control of Protein Orientation

A contribuição do mecanismo de transferência de carga para o efeito SERS em interfaces eletroquímicas

R aman Spectroelectrochemistry

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