X-ray structures of the peridinin-chlorophyll-protein reconstituted with different chlorophylls

Tim Schulte, Roger G. Hiller, Eckhard Hofmann*

*Corresponding author for this work

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The peridinin-chlorophyll a-protein (PCP) from dinoflagellates is a soluble light harvesting antenna which gathers incoming photons mainly by the carotenoid peridinin. In PCPs reconstituted with different chlorophylls, the peridinin to chlorophyll energy transfer rates are well predicted by a Förster-like theory, but only if the pigment arrangements are identical in all PCPs. We have determined the X-ray structures of PCPs reconstituted with Chlorophyll-b (Chl-b), Chlorophyll-d (Chl-d) and Bacteriochlorophyll-a (BChl-a) to resolutions ≤2 Å. In all three cases the pigment arrangements are essentially the same as in native PCP. Hydrogen bonding is not responsible for preferential incorporation of "non-native" chlorophylls over Chl-a.

Original languageEnglish
Pages (from-to)973-978
Number of pages6
JournalFEBS Letters
Volume584
Issue number5
DOIs
Publication statusPublished - 5 Mar 2010

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