Light-harvesting complexes of Botryococcus braunii

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The colonial green alga Botryococcus braunii (BB) is a potential source of biofuel due to its natural high hydrocarbon content. Unfortunately, its slow growth limits its biotechnological potential. Understanding its photosynthetic machinery could help to identify possible growth limitations. Here, we present the first study on BB light-harvesting complexes (LHCs). We purified two LHC fractions containing the complexes in monomeric and trimeric form. Both fractions contained at least two proteins with molecular weight (MW) around 25 kDa. The chlorophyll composition is similar to that of the LHCII of plants; in contrast, the main xanthophyll is loroxanthin, which substitutes lutein in most binding sites. Circular dichroism and 77 K absorption spectra lack typical differences between monomeric and trimeric complexes, suggesting that intermonomer interactions do not play a role in BB LHCs. This is in agreement with the low stability of the BB LHCII trimers as compared to the complexes of plants, which could be related to loroxanthin binding in the central (L1 and L2) binding sites. The properties of BB LHCII are similar to those of plant LHCII, indicating a similar pigment organization. Differences are a higher content of red chlorophyll a, similar to plant Lhcb3. These differences and the different Xan composition had no effect on excitation energy transfer or fluorescence lifetimes, which were similar to plant LHCII.

Original languageEnglish
Pages (from-to)191-201
Number of pages11
JournalPhotosynthesis Research
Volume135
Issue number1-3
DOIs
Publication statusPublished - 1 Mar 2018

Fingerprint

light harvesting complex
Light
Binding Sites
Xanthophylls
Lutein
lutein
Biofuels
Excitation energy
Chlorophyll
Algae
binding sites
Hydrocarbons
Chemical analysis
Pigments
Energy transfer
Machinery
Absorption spectra
circular dichroism spectroscopy
chlorophyll
Fluorescence

Keywords

  • Botryococcus braunii
  • LHC
  • Light-harvesting
  • Loroxanthin
  • Pigment-protein complexes

Cite this

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title = "Light-harvesting complexes of Botryococcus braunii",
abstract = "The colonial green alga Botryococcus braunii (BB) is a potential source of biofuel due to its natural high hydrocarbon content. Unfortunately, its slow growth limits its biotechnological potential. Understanding its photosynthetic machinery could help to identify possible growth limitations. Here, we present the first study on BB light-harvesting complexes (LHCs). We purified two LHC fractions containing the complexes in monomeric and trimeric form. Both fractions contained at least two proteins with molecular weight (MW) around 25 kDa. The chlorophyll composition is similar to that of the LHCII of plants; in contrast, the main xanthophyll is loroxanthin, which substitutes lutein in most binding sites. Circular dichroism and 77 K absorption spectra lack typical differences between monomeric and trimeric complexes, suggesting that intermonomer interactions do not play a role in BB LHCs. This is in agreement with the low stability of the BB LHCII trimers as compared to the complexes of plants, which could be related to loroxanthin binding in the central (L1 and L2) binding sites. The properties of BB LHCII are similar to those of plant LHCII, indicating a similar pigment organization. Differences are a higher content of red chlorophyll a, similar to plant Lhcb3. These differences and the different Xan composition had no effect on excitation energy transfer or fluorescence lifetimes, which were similar to plant LHCII.",
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Light-harvesting complexes of Botryococcus braunii. / van Den Berg, Tomas E.; van Oort, Bart; Croce, Roberta.

In: Photosynthesis Research, Vol. 135, No. 1-3, 01.03.2018, p. 191-201.

Research output: Contribution to JournalArticleAcademicpeer-review

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