Raman spectra of chlorophyll forms

Koyama, Yasushi; Umemoto, Yasuhiro; Akamatsu, Atsuko; Uehara, Kaku; Tanaka, Makoto

doi:10.1016/0022-2860(86)80299-x

Cited by 98 publications

(110 citation statements)

References 27 publications

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“…/P spectra, making the assignment difficult. The C=O frequency in each frequency region provides information of a hydrogen bond interaction and the polarity of the microenvironment; a lower frequency reflects stronger hydrogen bonding and higher polarity (Bekárek et al 1979;Koyama et al 1986;Krawczyk 1989). The frequencies of these C=O groups upshift upon cation formation and downshift upon triplet formation (Breton 2001;Breton and Nabedryk 1993;Mäntele et al 1988;Nabedryk 1996;Noguchi et al 1993;Okubo et al 2007).…”

Section: Light-induced Ftir Difference Spectra Of Special Pair (B)chlsmentioning

confidence: 94%

Fourier transform infrared spectroscopy of special pair bacteriochlorophylls in homodimeric reaction centers of heliobacteria and green sulfur bacteria

Noguchi

2010

Photosynth Res

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Heliobacteria and green sulfur bacteria have type I homodimeric reaction centers analogous to photosystem I. One remaining question regarding these homodimeric reaction centers is whether the structures and electron transfer reactions are truly symmetric or not. This question is relevant to the origin of the heterodimeric reaction centers, such as photosystem I and type II reaction centers. In this mini-review, Fourier transform infrared studies on the special pair bacteriochlorophylls, P798 in heliobacteria and P840 in green sulfur bacteria, are summarized. The data are reinterpreted in the light of the X-ray crystallographic structure of photosystem I and the sequence alignments of type I reaction center proteins, and discussed in terms of hydrogen bonding interactions and the symmetry of charge distribution over the dimer.

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Section: Light-induced Ftir Difference Spectra Of Special Pair (B)chlsmentioning

confidence: 94%

Fourier transform infrared spectroscopy of special pair bacteriochlorophylls in homodimeric reaction centers of heliobacteria and green sulfur bacteria

Noguchi

2010

Photosynth Res

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“…Raman spectra obtained from BChls from green photosynthetic bacteria are similar to those of the water-soluble Bchl-protein complexes but differ from spectra of monomeric and aggregated Bchls in vitro (58,59). Fourier transform (FT) Raman spectroscopy using 1,064-nm laser excitation permits one to obtain Raman spectra suppressing the accompanying Bchl fluorescence emission; thus, key Raman band signatures of the chlorophyll porphyrin skeletal vibrations could be assigned, which can be used to identify chlorophylls in complex cultures (60). The conjugated aromatic pyrrole rings coordinated with the central magnesium(II) ion give characteristic Raman bands in the region of 400 to 1,600 cm Ϫ1 , and these features have been adopted to identify the presence of chlorophylls in microbial colonies inhabiting rocks in cold-, UV-, and drought-stressed environments (61)(62)(63).…”

Section: Raman Spectrometry Of Microbial Pigments-pure Culture Studiesmentioning

confidence: 99%

Raman Spectroscopy of Microbial Pigments

Jehlička

Edwards

Oren

2014

Appl Environ Microbiol

143

114

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Raman spectroscopy is a rapid nondestructive technique providing spectroscopic and structural information on both organic and inorganic molecular compounds. Extensive applications for the method in the characterization of pigments have been found. Due to the high sensitivity of Raman spectroscopy for the detection of chlorophylls, carotenoids, scytonemin, and a range of other pigments found in the microbial world, it is an excellent technique to monitor the presence of such pigments, both in pure cultures and in environmental samples. Miniaturized portable handheld instruments are available; these instruments can be used to detect pigments in microbiological samples of different types and origins under field conditions.

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“…Thus, the spectrum contains only bands caused by the chromophore. The technique has contributed considerably to our understanding of the mechanism of retinal proteins and to the investigation of chromophore-protein interaction in proteins containing heme, bilin, chlorophyll, and carotenoid chromophores (1)(2)(3)(4)(5)(6). There are only a few, but in some cases severe, drawbacks to this method, which can make its application difficult.…”

mentioning

confidence: 99%

Fourier-transform Raman spectroscopy applied to photobiological systems.

Sawatzki

Fishcer

Scheer

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

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Fluorescence and initiation of photoreactions are problems frequently encountered with resonance Raman spectroscopy of photobiological systems. These problems can be circumvented with Fourier-transform Raman spectroscopy by using the 1064-nm wavelength of a continuous wave neodymium-yttrium/aluminum-garnet laser as the probing beam. This wavelength is far from the absorption band of most pigments. Yet, the spectra of the investigated systemsbacteriorhodopsin, rhodopsin, and phycocyanin-show that these systems are still dominated by the chromophore, or that preresonant Raman scattering is still prevalent. Only for rhodopsin were contributions of the protein and the membrane discernible. The spectra of phycocyanin differ considerably from those obtained by excitation into the UV-absorption band. The results show the usefulness of this method and its wide applicability. In addition, analysis of the relative preresonant scattering cross sections may provide a detailed insight into the scattering mechanism.Resonance Raman spectroscopy is a powerful technique for selectively studying chromophores in biological systems. By tuning the probing laser beam to the electronic transition of the chromophore(s) within the biological matrix (protein, lipids, etc.), the resonance-enhancement effect increases the scattering from the chromophore by several orders of magnitude. Thus, the spectrum contains only bands caused by the chromophore. The technique has contributed considerably to our understanding of the mechanism of retinal proteins and to the investigation of chromophore-protein interaction in proteins containing heme, bilin, chlorophyll, and carotenoid chromophores (1-6). There are only a few, but in some cases severe, drawbacks to this method, which can make its application difficult. Because the probing beam excites the chromophore into a higher electronic state, strong fluorescence may override the weaker spontaneous Raman scattering, making it undetectable against the fluorescence background. In active photobiological systems, the strong probing beam also initiates photoreaction(s), and special techniques must be applied to control the state of the system under investigation. This last point may become especially severe for systems in which the photoreaction is not reversible (i.e., systems that "bleach," such as vertebrate visual pigments) or in which the back-reaction is very slow (such as dark adaptation of bacteriorhodopsin or reversion of phytochrome). By pumping the sample through a capillary jet, the accumulation of the bleached state or of long-lived intermediates can be avoided, but large amounts of material are usually required.For a long time, analyzing the Raman-scattered light by a Fourier-transform (FT) spectrophotometer, or FT-Raman spectroscopy, was thought to have disadvantages as compared with conventional Raman spectroscopy (7-9). However, about 2 years ago, it was realized that by using a near-infrared laser, such as a neodymium-yttrium/aluminum-garnet (Nd:YAG) laser, as the probing beam, t...

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Raman spectra of chlorophyll forms

Cited by 98 publications

References 27 publications

Fourier transform infrared spectroscopy of special pair bacteriochlorophylls in homodimeric reaction centers of heliobacteria and green sulfur bacteria

Fourier transform infrared spectroscopy of special pair bacteriochlorophylls in homodimeric reaction centers of heliobacteria and green sulfur bacteria

Raman Spectroscopy of Microbial Pigments

Fourier-transform Raman spectroscopy applied to photobiological systems.

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