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

Eckhard Hofmann, Pamela M. Wrench, Frank P. Sharples, Roger G. Hiller, Wolfram Welte*, Kay Diederichs

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

359 Citations (Scopus)

Abstract

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 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.

Original languageEnglish
Pages (from-to)1788-1791
Number of pages4
JournalScience
Volume272
Issue number5269
DOIs
Publication statusPublished - 21 Jun 1996

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