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A protochlorophyllide light-harvesting complex involved in de-etiolation of higher plants

Abstract

When etiolated angiosperm seedlings break through the soil after germination, they are immediately exposed to sunlight, but at this stage they are unable to perform photosynthesis1. In the absence of chlorophyll a and chlorophyll b, two other porphyrin species cooperate as the basic light-harvesting structure of etiolated plants. Protochlorophyllide a and protochlorophyllide b (ref. 2) form supramolecular complexes with NADPH and two closely related NADPH:protochlorophyllide oxidoreductase (POR) proteins—PORA and PORB (ref. 3)—in the prolamellar body of etioplasts. Here we report that these light-harvesting POR–protochlorophyllide complexes, named LHPP, are essential for the establishment of the photosynthetic apparatus and also confer photoprotection on the plant. They collect sunlight for rapid chlorophyll a biosynthesis and, simultaneously, dissipate excess light energy in the bulk of non-photoreducible protochlorophyllide b. Based on this dual function, it seems that LHPP provides the link between skotomorphogenesis and photosynthesis that is required for efficient de-etiolation.

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Figure 1: Authentic LHPP contains two POR proteins but only one photoactive species of Pchlide.
Figure 2: PORA and PORB bind ZnPPa and ZnPPb, the Zn analogues of Pchlide a and Pchlide b, with different affinities.
Figure 3: Reconstitution of LHPP in vitro.
Figure 4: Reconstituted LHPP catalyses the reduction of ZnPPa to Zn pheophorbide a.
Figure 5: Reconstituted LHPP is a light-harvesting complex, collecting solar energy for the formation of PORB-derived Zn pheophorbide a.
Figure 6: Mixed galacto- and sulpholipids promote the formation of Pchlide650–657 in reconstituted LHPP.

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Acknowledgements

We thank S. Schoch for a gift of ZnPPa and ZnPPb. This work is dedicated to R.Mache on the occasion of his 65th birthday.

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Correspondence to Christiane Reinbothe.

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Reinbothe, C., Lebedev, N. & Reinbothe, S. A protochlorophyllide light-harvesting complex involved in de-etiolation of higher plants. Nature 397, 80–84 (1999). https://doi.org/10.1038/16283

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