Energy level diagram showing relationship between Rayleigh, Raman, and resonance Raman scattering and fluorescence.
Resonance Raman spectroscopy (RR spectroscopy or RRS) is a variant of Raman spectroscopy in which the incident photon energy is close in energy to an electronic transition of a compound or material under examination.[1] This similarity in energy (resonance) leads to greatly increased intensity of the Raman scattering of certain vibrational modes, compared to ordinary Raman spectroscopy.
Resonance Raman spectroscopy has much greater sensitivity than non-resonance Raman spectroscopy, allowing for the analysis of compounds with inherently weak Raman scattering intensities, or at very low concentrations.[2][3] It also selectively enhances only certain molecular vibrations (those of the chemical group undergoing the electronic transition), which simplifies spectra.[3] For large molecules such as proteins, this selectivity helps to identify vibrational modes of specific parts of the molecule or protein, such as the heme unit within myoglobin.[4] Resonance Raman spectroscopy has been used in the characterization of inorganic compounds and complexes,[5] proteins,[6][7] nucleic acids,[8] pigments,[8] and in archaeology and art history.[8]
^Strommen, Dennis P.; Nakamoto, Kazuo (1977). "Resonance raman spectroscopy". Journal of Chemical Education. 54 (8): 474. Bibcode:1977JChEd..54..474S. doi:10.1021/ed054p474. ISSN 0021-9584.
^Drago, R.S. (1977). Physical Methods in Chemistry. Saunders. p. 152.
^ abMorris, Michael D.; Wallan, David J. (1979). "Resonance raman spectroscopy: Current applications and prospects". Analytical Chemistry. 51 (2): 182A–192A. doi:10.1021/ac50038a001. ISSN 0003-2700.
^Hu, Songzhou; Smith, Kevin M.; Spiro, Thomas G. (January 1996). "Assignment of Protoheme Resonance Raman Spectrum by Heme Labeling in Myoglobin". Journal of the American Chemical Society. 118 (50): 12638–46. doi:10.1021/ja962239e.
^Clark, Robin J.H.; Dines, Trevor J. (February 1986). "Resonance Raman spectroscopy, and its application to inorganic chemistry". Angewandte Chemie International Edition. 25 (2): 131–158. doi:10.1002/anie.198601311. ISSN 0570-0833.
^Austin, J.C.; Rodgers, K.R.; Spiro, T.G. (1993). Protein Structure from ultraviolet resonance Raman spectroscopy. Methods in Enzymology. Vol. 226. pp. 374–396. doi:10.1016/0076-6879(93)26017-4. PMID 8277873.
^Spiro, T.G.; Czernuszewicz, R.S. (1995). Resonance Raman spectroscopy of metalloproteins. Methods in Enzymology. Vol. 246. pp. 416–460. doi:10.1016/0076-6879(95)46020-9. ISSN 0076-6879. PMID 7752933.
^ abcEfremov, Evtem V.; Ariese, Freek; Gooijer, Cees (2008). "Achievements in resonance Raman spectroscopy: Review of a technique with a distinct analytical chemistry potential". Analytica Chimica Acta. 606 (2): 119–134. doi:10.1016/j.aca.2007.11.006. PMID 18082644.
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