Spectroscopy of Biliproteins and Energy Transfer in Photosynthetic Antenna Complexes

Schneider, Siegfried

doi:10.1007/978-94-011-2698-4_13

Cited by 2 publications

(2 citation statements)

References 17 publications

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“…The latter band is clearly seen only in the spectrum covering the region from 1250-1400 cm-' (an explanation for why it is not seen in the first section is given below). It is worth mentioning that the band observed at 1232 cm-I in PC trimers is assigned to the a-chromophore because at this frequency a band appears only in the a-subunit, but not in the P-subunit (10,20). Therefore, the strong band at 1235 cm-I observed in the 585 nm spectrum of PEC should originate from that part of the PVB chromophore that is essentially the same as in the PCB chromophore (rings B-C-D fragment).…”

Section: Native Samples Without H/d Exchangementioning

confidence: 99%

Resonance‐Enhanced CARS Spectroscopy of Biliproteins: a Comparison Between Phycoerythrocyanin and Phycocyanin of Mastigocladus laminosus

Schneider

Prenzel

Brehm

et al. 1996

Photochem & Photobiology

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Abstract— Resonance‐enhanced coherent anti‐Stokes Raman (CARS) spectra are reported for trimers of phycoerthrocyanin (PEC) dissolved in H2O and D2O. The CARS spectra are significantly different when recorded with pump wavelength either at 585 nm or 630 nm. By comparison of the 630 nm spectra with those of phycocyanin one can conclude that there is a change in the relative location of the lowest excited states of the β84 and β155 chromophores. Upon additional illumination with 514.5 nm laser light, only the spectra recorded with 585 nm pump wavelength change. This is in accordance with earlier observations that the phycoviolobilin chromophore of the a‐subunit exhibits photochromic behavior. The changes in the CARS spectra provide evidence that it is the methine bridge between rings C and D that undergoes the geometrical changes. Furthermore, it is suggested that there are different types of photoinduced rearrangements operative and that the isomeric distribution is different in H2O and D2O.

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Section: Native Samples Without H/d Exchangementioning

confidence: 99%

Resonance‐Enhanced CARS Spectroscopy of Biliproteins: a Comparison Between Phycoerythrocyanin and Phycocyanin of Mastigocladus laminosus

Schneider

Prenzel

Brehm

et al. 1996

Photochem & Photobiology

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“…Such microheterogeneity is also being discussed for other biliproteins, e.g. phycocyanin (Schneider, 1992). Heterogeneity of phytochrome has also been investigated by fluorescence of Pr at low temperature.…”

Section: Heterogeneity Of the Phototransformationmentioning

confidence: 99%

Events in the Phytochrome Molecule After Irradiation

Rüdiger¹

1992

Photochem & Photobiology

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Abstract-The photoconversion of Pr to Pfr has been investigated by a large number of investigators. We have previously demonstrated that Z,E isomerization of the tetrapyrrole chromophore is involved in the photoconversion. It is the best candidate for the primary photoreaction. Conformation and configuration of the Pr chromophore will be compared with that of chromophores in phycocyanin. The crystal structure of phycocyanin had been elucidated by x-ray analysis. Proton transfer and/or Z, E isomerization of the tetrapyrrole are probably involved in different steps of the photoconversion in phytochrome and in photoreversible phycobiliproteins. Fluorescence decay kinetics of irradiated Pr and intermediate formation show heterogeneity. Possible reasons for this heterogeneity will be discussed. Pisum sativum L.

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Spectroscopy of Biliproteins and Energy Transfer in Photosynthetic Antenna Complexes

Cited by 2 publications

References 17 publications

Resonance‐Enhanced CARS Spectroscopy of Biliproteins: a Comparison Between Phycoerythrocyanin and Phycocyanin of Mastigocladus laminosus

Resonance‐Enhanced CARS Spectroscopy of Biliproteins: a Comparison Between Phycoerythrocyanin and Phycocyanin of Mastigocladus laminosus

Events in the Phytochrome Molecule After Irradiation

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