Investigation of the SERS behaviour of porphyrins with different surface concentrations on electrochemically prepared Ag-surface.

Surface-enhanced Raman scattering (SERS) spectra, taken with 632.8 nm excitation are reported for the water-soluble tetrakis(3-N-methylpyridyl)porphyrin chloride (TMPyP(3)), tetrakis(4-N-methylpyridyl)porphyrin chloride (TMPyP(4)) and Sn(IV)tetrakis(4-N-methylpyridyl)porphyrin chloride (Sn(IV)TMPyP(4)) using an electrochemically prepared Ag surface with an area ca. 12.56 mm2. It was found that the spectra vary as increasing amounts of the compounds are placed on the surface, with surface concentrations in the approximate range 1000-5 pmol/12.56 mm2. We suggest that the reasons for the changes be that the reaction means between porphyrin molecules and Ag surface is different and the porphyrin macrocyclic molecules adopt different orientation as the surface concentrations decrease.

Vibrational spectroscopic study of the contents of a chest excavated from the wreck of the HMS Pandora.

The FT-IR and Raman spectroscopic analysis of a red powder found in a chest from an officer's cabin during the excavation of the wreck of the 18th Century frigate HMS Pandora have confirmed that the pigment is cinnabar, mercury(II) sulphide. Weaker signals in the Raman spectrum are assignable to a proteinaceous material, such as collagen, typical of a degraded vellum or parchment. Comparison of the Raman spectra with that of a pigmented seal from a 1786 Lieutenant's commission demonstrated that the beeswax component of the seal was not observable.

[The effect of temperature on the behavior of aminobenzoic acid on silver surface].

SERS spectra of p-Aminobenzoic Acid (PABA) and o-Aminobenzoic Acid (OABA) absorbed on a silver surface, roughened by nitric acid, have been measured with a Renishaw Raman microprobe spectrometer(lambda = 632.8 nm) at different temperature, which ranged from 30 degrees C to -190 degrees C and from -190 degrees C to 30 degrees C. Some reversible changes in some band positions have been observed. The results indicated that if the adsorbates were enhanced by chemical mechanism and the molecules lie flat on surface, e.g. p-Aminobenzoic Acid molecule, temperature had no effect on their orientation. However, the vibrational frequencies enhanced by electromagnetic mechanism shifted as temperature changed, e.g. the vibration of NH2 in o-Aminobenzoic. The fact was that temperature had effect on the orientation of the molecules.

[Reversible temperature dependence of surface-enhanced Raman scattering of adenine, purine and pyrene].

The surface-enhanced Raman scattering (SERS) spectra of adenine, purine and pyrene adsorbed on a SERS-active silver surface roughened by nitric acid have been measured over the -190 degrees C-30 degrees C surface temperature range. The results show that the Raman shifts and SERS intensity of the vibrations, which are enhanced by electromagnetic mechanism, are affected by temperature, those by chemical mechanism are not. However, it has been found that the observed temperature dependence can be explained by postulating the reorientation of the absorbates. Adenine molecules and purine molecules prefer to adopt a more perpendicular stance on the surface at high temperature, but for a planar symmetric molecule, such as pyrene, the preferred orientation is parallel and temperature has no effect on its orientation.

Keratin orientation in wool and feathers by polarized raman spectroscopy.

Good quality polarized Raman spectra of a single wool fiber and an intact feather barbule are presented. The intensity ratio of the alpha-helix component of the amide I band measured parallel and perpendicular to the wool fiber axis was 0.39 +/- 0.05. This is consistent with theoretical predictions based on orientational calculations using the normal Raman polarizability tensor for an alpha-helical amide I band where the protein strands are aligned roughly parallel with the fiber axis. However, the depolarized spectral intensity of the alpha-helix mode was greater than expected. For the feather barbule, despite high quality spectra, a unique orientation of the beta-sheet structure could not be determined using the Raman intensity ratios of the amide I band alone. Using previously developed methods, the protein chains were found to be oriented between 60 and 90 degrees from the long axis of the barbule compared to an angle of 51 degrees calculated from polarized IR spectra of the same barbule. The Raman tensor methods for the determination of protein orientation in these fibers was found to be constrained by the complexity of the materials and the limitations of the band fitting methods used to apportion the intensity among the various vibrational modes of their spectra. Other advantages and limitations of polarized Raman microscopic methods of structural determination are discussed.