Structural basis of light harvesting by carotenoids : peridinin-chlorophyll-protein from Amphidinium carterae

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1996
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Hofmann, Eckhard
Wrench, Pamela M.
Sharples, Frank P.
Hiller, Roger G.
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Science. 1996, 272(5269), pp. 1788-1791. ISSN 0036-8075. eISSN 1095-9203. Available under: doi: 10.1126/science.272.5269.1788
Zusammenfassung

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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570 Biowissenschaften, Biologie
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ISO 690HOFMANN, 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.272.5269.1788
BibTex
@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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