Raman difference spectorscopy

Bodenheimer, J.; Berenblut, B.J.; Wilkinson, Geoffrey

doi:10.1016/0009-2614(72)80257-4

Cited by 29 publications

(6 citation statements)

References 2 publications

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“…Description of Former Devices and Progress in Instrumentation. Raman difference spectroscopy was introduced by Bodenheimer et al in 1972 . They pointed out for the first time the usefulness of this comparison technique by cancelling out signals common to both samples, thus facilitating the observation of certain effects, like small wavenumber shifts or the detection of minor components.…”

Section: Resultsmentioning

confidence: 99%

“…The advantages of this resonance effect in terms of increased sensitivity as well as selectivity were especially successfully demonstrated for biological samples. − The thermal decomposition of the absorbing samples, because of a strong local heating, can be avoided by means of the rotating sample technique. , Wavenumber shifts Δν caused by small structural differences (e.g., because of weak interactions with the solvent) are often below 1 cm -1 ; however, the limit in detection of frequency shifts between two spectra is ∼1−3 cm -1 due to the irreproducibility of conventional spectrometers. This limitation can be overcome by the application of the Raman difference spectroscopy (RDS) technique. , Small wavenumber shifts between two Raman signals can be calculated from the difference spectra with a precision down to ∼1/100 of Γ, the full width at half-maximum of the Raman band. This valuable increase in precision is possible as long as the Raman band itself is wider than one element of the detector.…”

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confidence: 99%

“… For a given line shape ( F , Γ) and intensity I 0 , the Raman shift Δν is determined by d and, therefore, by the intensity magnitudes in the difference signal. The RDS method can also be applied for the accurate determination of band broadening and also for obtaining a higher sensitivity in detecting minor sample components (by suppressing unwanted signals, e.g., from the solvent). , …”

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Device for Raman Difference Spectroscopy

et al. 2007

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A new layout of a versatile Raman difference setup is presented. The new device combines the advantages of the rotating cell for exploitation of the resonance Raman enhancement and the high precision of Raman difference spectroscopy together with the multiplex advantages and very high quantum efficiency offered by a CCD detector. While Raman difference spectroscopy is the most accurate method for the detection of very small band shifts, the method requires the strict prevention of any environmental perturbation of one of the two spectra, which are used for the difference spectra calculation. The presented device satisfies this requirement by implementing a double-beam layout, where the simultaneously detected Raman signals of two sample cells are combined within a Y-fiber bundle and imaged together onto the CCD detector. The accuracy of the new apparatus in detecting frequency shifts and minor sample components is greatly increased compared to conventional Raman spectroscopy as shown by studying binary mixtures of CHCl3 and CCl4. Hereby it was possible to resolve a formerly undetected shift of <0.02 cm(-1) of the CCl4 band at 218 cm(-1). The new RDS setup has a very versatile design. The device can take advantage of the high sensitivity and selectivity of the resonance Raman enhancement applying excitation wavelengths from the UV to NIR and can be used for a variety of samples with only minor changes in the optical arrangement. The new device will be of utmost importance for a fast, gentle, sensitive, selective, and precise investigation of biomolecules and their interactions. Some first results are shown concerning the interaction of the antimalarial chloroquine with hematin in a hydrous environment.

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Device for Raman Difference Spectroscopy

et al. 2007

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“…Enzyme-substrate interactions are obvious examples. The idea of using classical Raman difference spectroscopy to obtain changes in a molecular spectrum resulting from small perturbation has been previously proposed (Bodenheimer et al, 1972;Kiefer, 1973). However, apart from our recent study (Yue et al, 1984b), the technique has not been applied to the studies of proteins.…”

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Classical Raman spectroscopic studies of NADH and NAD+ bound to liver alcohol dehydrogenase by difference techniques

Chen¹,

Yue²,

Martin³

et al. 1987

Biochemistry

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We report the Raman spectra of reduced and oxidized nicotinamide adenine dinucleotide (NADH and NAD+, respectively) and adenosine 5'-diphosphate ribose (ADPR) when bound to the coenzyme site of liver alcohol dehydrogenase (LADH). The bound NADH spectrum is calculated by taking the classical Raman difference spectrum of the binary complex, LADH/NADH, with that of LADH. We have investigated how the bound NADH spectrum is affected when the ternary complexes with inhibitors are formed with dimethyl sulfoxide (Me2SO) or isobutyramide (IBA), i.e., LADH/NADH/Me2SO or LADH/NADH/IBA. Similarly, the difference spectra of LADH/NAD+/pyrazole or LADH/ADPR with LADH are calculated. The magnitude of these difference spectra is on the order of a few percent of the protein Raman spectrum. We report and discuss the experimental configuration and control procedures we use in reliably calculating such small difference signals. These sensitive difference techniques could be applied to a large number of problems where the classical Raman spectrum of a "small" molecule, like adenine, bound to the active site of a protein is of interest. The spectrum of bound ADPR allows an assignment of the bands of the bound NADH and NAD+ spectra to normal coordinates located primarily on either the nicotinamide or the adenine moiety. By comparing the spectra of the bound coenzymes with model compound data and through the use of deuterated compounds, we confirm and characterize how the adenine moiety is involved in coenzyme binding and discuss the validity of the suggestion that the adenine ring is protonated upon binding. The nicotinamide moiety of NADH shows significant molecular changes upon binding.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…The factors influencing the precision of the measurement of polarization in Raman spectra have been discussed (37). Two methods for measuring difference spectra using single-beam instrumentation have been devised (38,39).…”

Section: Instrumentation and Sampling Techniquementioning

confidence: 99%

Raman spectrometry

Grossman¹

1974

Anal. Chem.

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This Review covers selected portions of the literature appearing between late 1971 and late 1973. Activity in the field has continued at a high level since the previous review in this series (1), and it seems neither possible nor desirable to give a comprehensive coverage of the published literature. The emphasis here will be on the chemical applications of Raman spectrometry, especially in the areas of analysis and instrumentation, as being most like-ly to be of interest to the readers of this journal. Where possible, reviews and other secondary sources which give more detailed coverage of smaller areas will be referenced.Several new books have appeared during the time covered by the review (2-7), evidence of the need for consolidation and ordering in a rapidly growing field. A critical compilation of vibrational frequencies of 55 polyatomic molecules has been published (8). Inorganic vibrational

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Raman difference spectorscopy

Cited by 29 publications

References 2 publications

Device for Raman Difference Spectroscopy

Device for Raman Difference Spectroscopy

Classical Raman spectroscopic studies of NADH and NAD+ bound to liver alcohol dehydrogenase by difference techniques

Raman spectrometry

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