Publikation: Structural basis of light harvesting by carotenoids : peridinin-chlorophyll-protein from Amphidinium carterae
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Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a bluegreen absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the α-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances.
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HOFMANN, Eckhard, Pamela M. WRENCH, Frank P. SHARPLES, Roger G. HILLER, Wolfram WELTE, Kay DIEDERICHS, 1996. Structural basis of light harvesting by carotenoids : peridinin-chlorophyll-protein from Amphidinium carterae. In: Science. 1996, 272(5269), pp. 1788-1791. ISSN 0036-8075. eISSN 1095-9203. Available under: doi: 10.1126/science.272.5269.1788BibTex
@article{Hofmann1996Struc-7302, year={1996}, doi={10.1126/science.272.5269.1788}, title={Structural basis of light harvesting by carotenoids : peridinin-chlorophyll-protein from Amphidinium carterae}, number={5269}, volume={272}, issn={0036-8075}, journal={Science}, pages={1788--1791}, author={Hofmann, Eckhard and Wrench, Pamela M. and Sharples, Frank P. and Hiller, Roger G. and Welte, Wolfram and Diederichs, Kay} }
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