Application of FT-Raman spectroscopy to the study of selected organometallic complexes and proteins
01 Jul 1990-Canadian Journal of Chemistry (NRC Research Press Ottawa, Canada)-Vol. 68, Iss: 7, pp 1196-1200
TL;DR: In this paper, the FT-Raman spectra of a series of arene chromium tricarbonyl complexes and of cyclopentadienyl manganese tricaronyl were obtained and assigned.
Abstract: The study of colored organometallic complexes by dispersive Raman spectroscopy has been limited due to fluorescence or photodecomposition caused by the visible laser used as the excitation source. As a solution to this problem, FT-Raman spectroscopy with a near-infrared laser source has been useful in lowering fluorescence or photolysis in these samples. To investigate the utility of this technique, we have obtained and assigned the FT-Raman spectra of a series of arene chromium tricarbonyl complexes and of cyclopentadienyl manganese tricarbonyl. Some bands previously unobserved by dispersive Raman spectroscopy were seen, including a band assigned to a 13CO satellite in the spectrum of methylbenzoate chromium tricarbonyl. In addition, FT-Raman data for bovine serum albumin (BSA) and Protein-A are presented. Keywords: FT-Raman spectroscopy, metal carbonyl, proteins, organometallics, near infrared.
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TL;DR: In this article, the metal ion environments in metalloproteins and metalloenzymes can be studied by resonance Raman (RR) spectroscopy, where the wavelength of the exciting laser line is adjusted to coincide with that of an allowed electronic transition in a molecule, the intensities of certain Raman bands are enhanced relative to the off-resonance values.
Abstract: Publisher Summary This chapter discusses how metal ion environments in metalloproteins and metalloenzymes can be studied by resonance Raman (RR) spectroscopy. The chapter describes experimental techniques and methods of analysis and interpretation by using selected examples. The ability of RR spectroscopy to identify the presence or absence of particular structural units, and the ligation modes of the amino acids, has made the technique especially powerful in studies of protein structure and function. The central advantage of RR spectroscopy is that, when the wavelength of the exciting laser line is adjusted to coincide with that of an allowed electronic transition in a molecule, the intensities of certain Raman bands are enhanced relative to the off-resonance values. The technique is therefore more sensitive than normal (off-resonance) Raman spectroscopy. Resonance Raman scattering occurs when a material is irradiated with monochromatic light corresponding to an allowed absorption band region. The effect is studied by examining the intensity of scattered photons as a function of the proximity of the excitation wavelength to electronic absorption bands of the molecule.
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TL;DR: In this paper, the infrared and Raman spectra of methyl and methoxy substituted benzene chromium tricarbonyl complexes (η6-C6H6−nXn)Cr(CO)3 are reported.
20 citations
TL;DR: In this paper , the authors compared differences between the spectroscopic spectra of individual compounds with the chemical structure for the flavonoids subgroups: flavones, isoflavones, flavanones and anthocyanins.
18 citations
TL;DR: In this paper, a sudy of a wide variety of coloured main group metal, transition metal coordination and transition metal organometallic complexes using Fourier transform Raman (FT-Raman) spectroscopy has demonstrated a high success rate ( ca 50%) with good quality spectra obtained in short periods of time.
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01 Jan 1995
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TL;DR: In this paper, a sudy of a wide variety of coloured main group metal, transition metal coordination and transition metal organometallic complexes using Fourier transform Raman (FT-Raman) spectroscopy has demonstrated a high success rate ( ca 50%) with good quality spectra obtained in short periods of time.
14 citations