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

Tim Schulte; Roger G. Hiller; Eckhard Hofmann

doi:10.1016/j.febslet.2010.01.041

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 journal › Article › peer-review

21 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 language	English
Pages (from-to)	973-978
Number of pages	6
Journal	FEBS Letters
Volume	584
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2010.01.041
Publication status	Published - 5 Mar 2010

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10.1016/j.febslet.2010.01.041

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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 F{\"o}rster-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 {\AA}. 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.",

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T1 - X-ray structures of the peridinin-chlorophyll-protein reconstituted with different chlorophylls

AU - Schulte, Tim

AU - Hiller, Roger G.

AU - Hofmann, Eckhard

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Y1 - 2010/3/5

N2 - 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.

AB - 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.

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U2 - 10.1016/j.febslet.2010.01.041

DO - 10.1016/j.febslet.2010.01.041

M3 - Article

C2 - 20102711

AN - SCOPUS:76749127987

SN - 0014-5793

VL - 584

SP - 973

EP - 978

JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

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

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