Surface resonance Raman spectroscopy

Bilayer structures have been prepared and investigated with various spectroelectrochemical techniques [307, 486]. In the former report, surface resonance Raman spectroscopy showed typical vibrational features of the involved polymers [PANI and poly(o-phenylenediamine] as already discussed were observed. In the latter investigation, involving PANI/poly(5-chlorine,2-metho3 ani-line), it was concluded that the topmost layer of the polymerized substituted aniline blocks the electrochemical reduction of the inner layer of PANI. This was first deduced from the diminished height of reduction peaks in the CV. Moreover, this was supported by in situ UV-vis spectra that showed typictil bands of oxidized PANI even after formal reduction of the film. 

Surface resonance Raman spectroscopy Surface Raman spectroscopy specular reflectance speetroscopy Scanning tunneling microscope Sinface-unenhanced Raman spectroscopy Soft X-ray appearance potential spectroscopy Soft X-ray emission spectroscopy Thermodesorption mass spectroscopy Thermal energy atom scattering Third harmonic generation Thin layer cell... 

SERS. A phenomenon that certainly involves the adsorbent-adsorbate interaction is that of surface-enhanced resonance Raman spectroscopy, or SERS. The basic observation is that for pyridine adsorbed on surface-roughened silver, there is an amazing enhancement of the resonance Raman intensity (see Refs. 124—128). More recent work has involved other adsorbates and colloidal... 

Plenary 3. Ronald E Hester et al, e-mail address reh York.ac.uk (SERS). Use of dioxane envelope to bring water insoluble cliromophores (chlorophylls) into contact with aqueous silver colloids for SERS enliancement. PSERRS— protected surface-enhanced resonance Raman spectroscopy . 

In most work on electrochemical systems, use is made of two effects that greatly enhance the Raman signals. One is resonance Raman spectroscopy (RRS), wherein the excitation wavelength corresponds to an electronic transition in an adsorbed molecule on an electrode surface. The other effect is surface-enhanced Raman spectroscopy (SERS), which occurs on certain surfaces, such as electrochemically roughened silver and gold. This effect, discovered by Fleischmann et al. (1974), yields enhancements of 10 to 10 . The vast majority of publications on Raman studies of electrochemical systems use SERS. The limitations of SERS are that it occurs on only a few metals and the mechanism of the enhancement is not understood. There is speculation that only a small part of the surface is involved in the effect. There is a very good review of SERS (Pemberton, 1991). 

Hildebrandt P., Stockburger M., Surface-enhanced resonance Raman-spectroscopy of rhodamine-6G adsorbed on colloidal silver, J. Phys. Chem. 1984 88 5935-5944. 

Koglin E., Sequaris J.M., Interaction of proflavine with DNA studied by colloid surface enhanced resonance Raman-spectroscopy, J. Molecular Struct. 1986 141 405-409. 

P. Corio, S.D.M. Brown, A. Marucci, M.A. Pimenta, K. Kneipp, and G. Dresselhaus, M.S. Dresselhaus, Surface-enhanced resonant Raman spectroscopy of single-wall carbon nanotubes adsorbed on silver and gold surfaces. Phys. Rev. B 61, 13202—13211 (2000). 

The goal of this chapter will be to provide an overview of the use of planar, optically resonant nanophotonic devices for biomolecular detection. Nanophotonics23 24 represents the fusion of nanotechnology with optics and thus it is proposed that sensors based on this technology can combine the advantages of each as discussed above. Although many of the issues are the same, we focus here on optical resonance rather than plasmonic resonance (such as is used in emerging local SPR and surface-enhanced Raman spectroscopy-based biosensors). 

The use of surface-enhanced resonance Raman spectroscopy (SERRS) as an identification tool in TLC and HPLC has been investigated in detail. The chemical structures and common names of anionic dyes employed as model compounds are depicted in Fig. 3.88. RP-HPLC separations were performed in an ODS column (100 X 3 mm i.d. particla size 5 pm). The flow rate was 0.7 ml/min and dyes were detected at 500 nm. A heated nitrogen flow (200°C, 3 bar) was employed for spraying the effluent and for evaporating the solvent. Silica and alumina TLC plates were applied as deposition substrates they were moved at a speed of 2 mm/min. Solvents A and B were ammonium acetate-acetic acid buffer (pH = 4.7) containing 25 mM tributylammonium nitrate (TBAN03) and methanol, respectively. The baseline separation of anionic dyes is illustrated in Fig. 3.89. It was established that the limits of identification of the deposited dyes were 10 - 20 ng corresponding to the injected concentrations of 5 - 10 /ig/ml. It was further stated that the combined HPLC-(TLC)-SERRS technique makes possible the safe identification of anionic dyes [150],... 

R.M. Seifar, M.A.F. Altelaar, RJ. Dijkstra, F. Ariese, U.A. Th. Brinkman and C. Gooijer, Surface-enhanced resonance Raman spectroscopy (SERRS) as an identification tool in column liquid chromatography. Anal. Chem., 72 (2000) 5718-5724. 

A variety of physical methods has been used to ascertain whether or not surface ruthenation alters the structure of a protein. UV-vis, CD, EPR, and resonance Raman spectroscopies have demonstrated that myoglobin [14, 18], cytochrome c [5, 16, 19, 21], and azurin [13] are not perturbed structurally by the attachment of a ruthenium complex to a surface histidine. The reduction potential of the metal redox center of a protein and its temperature dependence are indicators of protein structure as well. Cyclic voltammetry [5, 13], differential pulse polarography [14,21], and spectroelectrochemistry [12,14,22] are commonly used for the determination of the ruthenium and protein redox center potentials in modified proteins. 

Probing Metalloproteins Electronic absorption spectroscopy of copper proteins, 226, 1 electronic absorption spectroscopy of nonheme iron proteins, 226, 33 cobalt as probe and label of proteins, 226, 52 biochemical and spectroscopic probes of mercury(ii) coordination environments in proteins, 226, 71 low-temperature optical spectroscopy metalloprotein structure and dynamics, 226, 97 nanosecond transient absorption spectroscopy, 226, 119 nanosecond time-resolved absorption and polarization dichroism spectroscopies, 226, 147 real-time spectroscopic techniques for probing conformational dynamics of heme proteins, 226, 177 variable-temperature magnetic circular dichroism, 226, 199 linear dichroism, 226, 232 infrared spectroscopy, 226, 259 Fourier transform infrared spectroscopy, 226, 289 infrared circular dichroism, 226, 306 Raman and resonance Raman spectroscopy, 226, 319 protein structure from ultraviolet resonance Raman spectroscopy, 226, 374 single-crystal micro-Raman spectroscopy, 226, 397 nanosecond time-resolved resonance Raman spectroscopy, 226, 409 techniques for obtaining resonance Raman spectra of metalloproteins, 226, 431 Raman optical activity, 226, 470 surface-enhanced resonance Raman scattering, 226, 482 luminescence... 

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