ArticlePhotosynthesis research2018
Light-harvesting complexes of Botryococcus braunii.
Article in Photosynthesis research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- A bioprocess engineering approach for the production of hydrocarbons and fatty acids from green microalga under high cobalt concentration as the feedstock of high-grade biofuels.Biotechnology for biofuels and bioproducts · 2024Article
- Total Synthesis of Loroxanthin.Marine drugs · 2022Article
- Oxidative Stress- and Autophagy-Inducing Effects of PSI-LHCI fromBiotech (Basel (Switzerland)) · 2022Article
- The Loroxanthin Cycle: A New Type of Xanthophyll Cycle in Green Algae (Chlorophyta).Frontiers in plant science · 2022Article
- PSI of the Colonial AlgaPlant physiology · 2020Article
- Light Acclimation of the Colonial Green AlgaPlant physiology · 2019Article
- Comparative transcriptome analyses of oleaginousBiotechnology for biofuels · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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