Spectroscopy resonance Raman scattering

In this section we will discuss more conventional spectroscopies absorption, emission and resonance Raman scattering. These spectroscopies are generally measured under single frequency conditions, and therefore our... 

Band gaps in semiconductors can be investigated by other optical methods, such as photoluminescence, cathodoluminescence, photoluminescence excitation spectroscopy, absorption, spectral ellipsometry, photocurrent spectroscopy, and resonant Raman spectroscopy. Photoluminescence and cathodoluminescence involve an emission process and hence can be used to evaluate only features near the fundamental band gap. The other methods are related to the absorption process or its derivative (resonant Raman scattering). Most of these methods require cryogenic temperatures. 

Resonance Raman spectroscopy has been applied to studies of polyenes for the following reasons. The Raman spectrum of a sample can be obtained even at a dilute concentration by the enhancement of scattering intensity, when the excitation laser wavelength is within an electronic absorption band of the sample. Raman spectra can give information about the location of dipole forbidden transitions, vibronic activity and structures of electronically excited states. A brief summary of vibronic theory of resonance Raman scattering is described here. 

In resonant Raman spectroscopy, the frequency of the incident beam is resonant with the energy difference between two real electronic levels and so the efficiency can be enhanced by a factor of 10 . However, to observe resonant Raman scattering it is necessary to prevent the possible overlap with the more efficient emission spectra. Thus, Raman experiments are usually realized under nonresonant illumination, so that the Raman spectrum cannot be masked by fluorescence. 

The metaiioporphyrins form a diverse class of molecules exhibiting complex and varied photochemistries. Until recently time-resolved absorption and fluorescence spectroscopies were the only methods used to study metailoporphyrln excited state relaxation in a submicrosecond regime. In this paper we present the first picosecond time-resolved resonance Raman spectra of excited state metaiioporphyrins outside of a protein matrix. The inherent molecular specificity of resonance Raman scattering provides for a direct probe of bond strengths, geometries, and ligation states of photoexcited metaiioporphyrins. 

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... 

S S CONTENTS Preface, C. Allen Bush. Methods in Macromo-lecular Crystallography, Andrew J. Howard and Thomas L. Poulos. Circular Dichroism and Conformation of Unordered Polypeptides, Robert W. Woody. Luminescence Studies with Horse Liver Dehydrogenase Information on the Structure, Dynamics, Transitions and Interactions of this Enzyme, Maurice R. Eftink. Surface-Enhanced Resonance Raman Scattering (SERRS) Spectroscopy A Probe of Biomolecular Structure and Bonding at Surfaces, Therese M. Cotton, Jae-Ho Kim and Randall E. Holt. Three-Dimensional Conformations of Complex Carbohydrates, C. Allen Bush and Perse-veranda Cagas. Index. 

The Raman scattering strength of E,(LO) in the vicinity of the fundamental bandgap has been investigated in resonant Raman scattering as a function of temperature between 77 K and 870 K [35], Studies of photocarrier thermalisation have been performed by time resolved Raman spectroscopy [36],... 

There has been tremendous work performed in molecular spectroscopy of biochemical and biological spectroscopy applying resonance Raman scattering. Several aspects have been discussed in detail by experts in the field. Spiro and Loehr (1975) have been one of the first researchers to summarize achievements made in the observation of res-... 

Sonnich Mortensen O, Massing S (1980) Polarization and interference phenomena in resonance Raman scattering. In Clark RJH, Hester RE (eds) Advances in Infrared and Raman spectroscopy, vol 6. Heyden and Sons, New York Soper SA, Ratzloff KL, Kuwana T (1990) Anal Chem 62 1438... 

Gomez-De Arco L, Lei B, Cronin BS, Zhou C (2008) Resonant micro-Raman spectroscopy of aligned single-walled carbon nanotubes on a-plane sapphire. Appl Phys Lett 93 123112 Jorio A, Pimenta MA, Souza Filho AG, Saito R, Dresselhaus G, Dresselhaus MS (2003) Characterizing carbon nanotube samples with resonance Raman scattering. New J Phys 5 139.1-139.17... 

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