Hole burning study of cyanobacterial Photosystem II complexes differing in the content of small putative chlorophyll-binding proteins. Dedic, R., Promnares, K., Psencik, J., Svoboda, A., Korinek, M., Tichy, M., Komenda, J., Funk, C., & Hala, J. Journal of Luminescence, 107(1-4):230–235, May, 2004. Place: Amsterdam Publisher: Elsevier WOS:000220706100031doi abstract bibtex This contribution presents low-temperature absorption, both broad-band and site-selective excited fluorescence, and persistent hole burning spectra of Photosystem II complexes from the Photosystem I-lacking strains of the cyanobacterium Synechocystis sp. PCC 6803 differing in the content of small putative chlorophyll-binding proteins (Scps). These proteins are homologous to light-harvesting complex of higher plants and may bind pigments. The excited state lifetimes of the complexes were determined from zero-phonon hole widths extrapolated to zero-burning dose. The area and spectral position of a phonon side-band with respect to the zero-phonon hole provided additional information concerning chlorophyll-protein coupling and the Stokes shift. Decrease of three absorption subbands at (670.0, 672.9, and 675.7 nm) in the Photosystem II isolated from the strain lacking ScpC and ScpD is in agreement with a hypothesis about the role of Scps in the chlorophyll binding. In addition, narrowing of the zero-phonon hole in Photosystem II without both Scps indicates slowering of the excitation energy transfer which may be explained by the absence of a protective excitation energy quenching related to the presence of Scps. (C) 2003 Elsevier B.V. All rights reserved.
@article{dedic_hole_2004,
title = {Hole burning study of cyanobacterial {Photosystem} {II} complexes differing in the content of small putative chlorophyll-binding proteins},
volume = {107},
issn = {0022-2313},
doi = {10/bvfqd3},
abstract = {This contribution presents low-temperature absorption, both broad-band and site-selective excited fluorescence, and persistent hole burning spectra of Photosystem II complexes from the Photosystem I-lacking strains of the cyanobacterium Synechocystis sp. PCC 6803 differing in the content of small putative chlorophyll-binding proteins (Scps). These proteins are homologous to light-harvesting complex of higher plants and may bind pigments. The excited state lifetimes of the complexes were determined from zero-phonon hole widths extrapolated to zero-burning dose. The area and spectral position of a phonon side-band with respect to the zero-phonon hole provided additional information concerning chlorophyll-protein coupling and the Stokes shift. Decrease of three absorption subbands at (670.0, 672.9, and 675.7 nm) in the Photosystem II isolated from the strain lacking ScpC and ScpD is in agreement with a hypothesis about the role of Scps in the chlorophyll binding. In addition, narrowing of the zero-phonon hole in Photosystem II without both Scps indicates slowering of the excitation energy transfer which may be explained by the absence of a protective excitation energy quenching related to the presence of Scps. (C) 2003 Elsevier B.V. All rights reserved.},
language = {English},
number = {1-4},
journal = {Journal of Luminescence},
author = {Dedic, R. and Promnares, K. and Psencik, J. and Svoboda, A. and Korinek, M. and Tichy, M. and Komenda, J. and Funk, C. and Hala, J.},
month = may,
year = {2004},
note = {Place: Amsterdam
Publisher: Elsevier
WOS:000220706100031},
keywords = {antenna complex, chlorophyll-protein interaction, cp 34, cyanobacteria, energy-transfer, hole burning, low-temperature, mutant, small cab like proteins},
pages = {230--235},
}
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These proteins are homologous to light-harvesting complex of higher plants and may bind pigments. The excited state lifetimes of the complexes were determined from zero-phonon hole widths extrapolated to zero-burning dose. The area and spectral position of a phonon side-band with respect to the zero-phonon hole provided additional information concerning chlorophyll-protein coupling and the Stokes shift. Decrease of three absorption subbands at (670.0, 672.9, and 675.7 nm) in the Photosystem II isolated from the strain lacking ScpC and ScpD is in agreement with a hypothesis about the role of Scps in the chlorophyll binding. In addition, narrowing of the zero-phonon hole in Photosystem II without both Scps indicates slowering of the excitation energy transfer which may be explained by the absence of a protective excitation energy quenching related to the presence of Scps. (C) 2003 Elsevier B.V. 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PCC 6803 differing in the content of small putative chlorophyll-binding proteins (Scps). These proteins are homologous to light-harvesting complex of higher plants and may bind pigments. The excited state lifetimes of the complexes were determined from zero-phonon hole widths extrapolated to zero-burning dose. The area and spectral position of a phonon side-band with respect to the zero-phonon hole provided additional information concerning chlorophyll-protein coupling and the Stokes shift. Decrease of three absorption subbands at (670.0, 672.9, and 675.7 nm) in the Photosystem II isolated from the strain lacking ScpC and ScpD is in agreement with a hypothesis about the role of Scps in the chlorophyll binding. In addition, narrowing of the zero-phonon hole in Photosystem II without both Scps indicates slowering of the excitation energy transfer which may be explained by the absence of a protective excitation energy quenching related to the presence of Scps. (C) 2003 Elsevier B.V. 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