Structural Basis of Light Harvesting by Carotenoids: Peridinin-Chlorophyll-Protein from <b> <i>Amphidinium carterae</i> </b>

DOI Web Site 被引用文献18件
  • Eckhard Hofmann
    E. Hofmann, W. Welte, K. Diederichs, Fakultät für Biologie, Universität Konstanz, Postfach 5560 (M656), 78434 Konstanz, Germany.
  • Pamela M. Wrench
    P. M. Wrench, F. P. Sharples, R. G. Hiller, School of Biological Sciences, Macquarie University, New South Wales 2109, Australia.
  • Frank P. Sharples
    P. M. Wrench, F. P. Sharples, R. G. Hiller, School of Biological Sciences, Macquarie University, New South Wales 2109, Australia.
  • Roger G. Hiller
    P. M. Wrench, F. P. Sharples, R. G. Hiller, School of Biological Sciences, Macquarie University, New South Wales 2109, Australia.
  • Wolfram Welte
    E. Hofmann, W. Welte, K. Diederichs, Fakultät für Biologie, Universität Konstanz, Postfach 5560 (M656), 78434 Konstanz, Germany.
  • Kay Diederichs
    E. Hofmann, W. Welte, K. Diederichs, Fakultät für Biologie, Universität Konstanz, Postfach 5560 (M656), 78434 Konstanz, Germany.

抄録

<jats:p> Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green 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 <jats:italic>a</jats:italic> 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. </jats:p>

収録刊行物

  • Science

    Science 272 (5269), 1788-1791, 1996-06-21

    American Association for the Advancement of Science (AAAS)

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