Chromophore states in allophycocyanin and phycocyanin. A resonance Raman study

Szalontai, Balázs; Gombos, Zoltán; Csizmadia, Vilmos; Csatorday, K.; Lutz, Marc

doi:10.1021/bi00441a046

Cited by 25 publications

(38 citation statements)

References 24 publications

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“…Note that in the FT-Raman spectra also, no carbonyl bands of the two lactam rings can be seen. However, considerable deviations are observed between the FT-Raman spectra and resonance Raman spectra, with excitation into the near-UV band (36,37). This result shows that (i) during the measurements performed by Margulies and Toporowicz (35) no degradation of the chromophore occurred and (it) care must be taken in comparing resonance Raman spectra of bile pigments obtained with excitation into different bands-e.g., the visible or UV absorption.…”

Section: Methodsmentioning

confidence: 96%

“…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.…”

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confidence: 99%

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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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Section: Methodsmentioning

confidence: 96%

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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“…Apparently, different modes are enhanced by the SERRS effect and by the ultraviolet excitation. Comparing the resonance Raman spectrum of phycocyanin with excitation in the visible band (Margulies and Toporowicz, 1988) with that obtained by excitation into the ultraviolet band (Szalontai et al, 1989), large deviations are apparent. Thus it appears that, for bilin pigments, the two types of resonance Raman spectra cannot be directly compared.…”

Section: Phytochromementioning

confidence: 93%

“…1 a), has been studied (Margulies and Stockburger, 1979;Margulies and Toporowicz, 1984), but this pigment differs from phytochrome by having a fully unsaturated chromophore system. Another model pigment is phycocyanin, a photosynthetic antenna pigment bearing a chromophore which is very similar to the one of phytochrome, and which has been investigated by resonance Raman (Szalontai et al, 1988;Szalontai et al, 1989;Margulies and Toporowicz, 1988), pre-resonance Raman (Sawatzki et al, 1990) and resonant coherent anti-Stokes Raman spectroscopy (CARRS) (Schneider et al, 1988a, b).…”

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confidence: 99%

Infrared spectroscopy of phytochrome and model pigments

Siebert

Grimm

Rüdiger

et al. 1990

European Journal of Biochemistry

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Fourier-transform infrared difference spectra between the red-absorbing and far-red-absorbing forms of oat phytochrome have been measured in H 2 0 and 2H20. The difference spectra are compared with infrared spectra of model compounds, i.e. the (52,102,152)-and (52,102,15E)-isomers of 2,3,7,8,12,13,17,18-octaethyl-bilindion (Et8-bilindion), 2,3-dihydro-2,3,7,8,12,13,17,18-octaethyl-bilindion (H2Et8-bilindion), and protonated H,Et8-bilindion in various solvents. The spectra of the model compounds show that only for the protonated forms can clear differences between the two isomers be detected. Since considerable differences are present between the spectra of Et8-bilindion and H2Et8-bilindion, it is concluded that only the latter compound can serve as a model system of phytochrome. The 2 H z 0 effect on the difference spectrum of phytochrome supports the view that the chromophore in red-absorbing phytochrome is protonated and suggests, in addition, that it is also protonated in far-red-absorbing phytochrome. The spectra show that protonated carboxyl groups are influenced. The small amplitudes in the difference spectra exclude major changes of protein secondary structure.

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“…Upon denaturation of the apoprotein, which causes the phycocyanobilin chromophore to adopt a more cyclic helical geometry, the above mentioned bands disappear and a new, strong band appears in the 162CL1630 cm-' region (Szalontai et al, 1987;Margulies and Toporowicz, 1984). That the chromophore's vibrational frequencies in the insect biliprotein approximate those of denatured phycocyanin can be taken as additional evidence for the cyclic helical structure.…”

Section: Discussionmentioning

confidence: 99%

BILIPROTEINS FROM THE BUTTERFLY Pieris brassicae STUDIED BY TIME‐RESOLVED FLUORESCENCE AND COHERENT ANTI‐STOKES RAMAN SPECTROSCOPY

Schneider¹,

Baumann²,

Geiselhart³

et al. 1988

Photochem & Photobiology

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Abstract-The fluorescence decay time of the biliverdin IXy chromophore present in biliproteins isolated from Pieris brassicae is determined to be 44 ? 3 ps. This value suggests a cyclic helical chromophore structure. The vibrational frequencies determined by CARS-spectroscopy are compared with those of model compounds. The data confirm that the chromophore in the protein-bound state adopts a cyclic-helical, flexible conformation.

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Chromophore states in allophycocyanin and phycocyanin. A resonance Raman study

Cited by 25 publications

References 24 publications

Fourier-transform Raman spectroscopy applied to photobiological systems.

Fourier-transform Raman spectroscopy applied to photobiological systems.

Infrared spectroscopy of phytochrome and model pigments

BILIPROTEINS FROM THE BUTTERFLY Pieris brassicae STUDIED BY TIME‐RESOLVED FLUORESCENCE AND COHERENT ANTI‐STOKES RAMAN SPECTROSCOPY

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