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

Schneider, Siegfried; Baumann, Fabian; Geiselhart, P.; Kayser, Hartmut; Scheer, Hugo

doi:10.1111/j.1751-1097.1988.tb02816.x

Cited by 6 publications

(1 citation statement)

References 16 publications

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“…in the native state of PC [2,11,12]. The semiextended and cyclic helical forms, present in the denatured state or some butterfly biliproteins [25], show fluorescence decay times which are much shorter.…”

Section: Mastigocladus Laminosus and Westiellopsis Prolificamentioning

confidence: 99%

Photophysics of phycoerythrocyanins from the cyanobacterium Westiellopsis prolifica studied by time-resolved fluorescence and coherent anti-Stokes Raman scattering spectroscopy

Schneider¹,

Jäger²,

Prenzel³

et al. 1994

Journal of Photochemistry and Photobiology B: Biology

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Three building blocks of the antenna complexes of the cyanobacterium Westiellopsis prolifica were studied: PEC(X), which is similar to the ot-subunit of phycoerythrocyanin (PEC), trimers of PEC and monomers derived from these by deaggregation with KSCN. The fit of the fluorescence decay curve of PEC(X) requires at least four exponentials, although it supposedly contains only one chromophore. The coherent anti-Stokes Raman scattering (CARS) spectra indicate that the heterogeneity observed is due to geometrical isomers, which are in part generated by photoinduced processes. A similar heterogeneity in chromophore structure and properties is also found in the monomers, where four exponentials are needed to fit the fluorescence decay curve. As in trimers, there is a long-lived, low-amplitude component, which can be assigned to impurities and/or oxidation products. The energy transfer time between the two phyocyanobilin chromophores in the/3-subunit is about 500 ps; the lifetime of the fluorescing /3-chromophore is 1.5 ns. The phycoviolobilin chromophore in the a-subunit adopts different geometries characterized by fluorescence liftetimes of about 240 and 800 ps. No evidence was found for energy transfer between the otehromophore and the /3-chromophores. This energy transfer occurs in trimers on a time scale of less than 20 ps; the energy transfer time between the two different types of/3-chromophore is about 250 ps and the lifetime of the terminal emitter is about 1.5 ns. The excited state kinetics are therefore similar to those of PEC trimers from Mastigocladus laminosus, as are the CARS spectra, indicating a similar chromophore-protein arrangement. In comparison with phycocyanin, the ordering of the excited states of chromophores fl84 and/3155 may be changed. Although PEC trimers of IVestiellopsis prolifica show almost as good a photostability as trimers of Mastigocladus laminosus, monomers are so photolabile that no CARS spectra could be recorded.

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Section: Mastigocladus Laminosus and Westiellopsis Prolificamentioning

confidence: 99%

Photophysics of phycoerythrocyanins from the cyanobacterium Westiellopsis prolifica studied by time-resolved fluorescence and coherent anti-Stokes Raman scattering spectroscopy

Schneider¹,

Jäger²,

Prenzel³

et al. 1994

Journal of Photochemistry and Photobiology B: Biology

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Resonance CARS spectroscopy of bile pigments from photosynthetic antennas

Baumann

Schneider

Gege

et al. 1989

Ber Bunsenges Phys Chem

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Resonance‐enhanced CARS spectra of various biliproteins (PBS**), PC**) and its β‐subunit, APC**)) from the cyanobacterium Mastigocladus laminosus are presented. It is concluded that upon desaggregation of the whole antenna complex (PBS) into trimeric APC and PC and of PC into its subunits the microheterogeneity of the chromophores increases. APC spectra recorded with different pump wavelengths show that one chromophore in APC adopts an extended, the other one a non‐extended geometry.

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Studies on biliprotein model compounds: Cars, picosecond time-resolved absorption and emission spectroscopy of a tryptophan-substituted 2,3-dihydro-bilatriene

Schneider

Geiselhart

Baumann

et al. 1988

Journal of Photochemistry and Photobiology B: Biology

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

Cited by 6 publications

References 16 publications

Photophysics of phycoerythrocyanins from the cyanobacterium Westiellopsis prolifica studied by time-resolved fluorescence and coherent anti-Stokes Raman scattering spectroscopy

Photophysics of phycoerythrocyanins from the cyanobacterium Westiellopsis prolifica studied by time-resolved fluorescence and coherent anti-Stokes Raman scattering spectroscopy

Resonance CARS spectroscopy of bile pigments from photosynthetic antennas

Studies on biliprotein model compounds: Cars, picosecond time-resolved absorption and emission spectroscopy of a tryptophan-substituted 2,3-dihydro-bilatriene

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