ArticlePhotosynthesis research2018
The structure of FCPb, a light-harvesting complex in the diatom Cyclotella meneghiniana.
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 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Structural and spectroscopic insights into fucoxanthin chlorophyll a/c-binding proteins of diatoms in diverse oligomeric states.Plant communications · 2024Article
- Lighting the way: Compelling open questions in photosynthesis research.The Plant cell · 2024Article
- Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII.Science advances · 2023Article
- A kaleidoscope of photosynthetic antenna proteins and their emerging roles.Plant physiology · 2022Article
- Revealing the architecture of the photosynthetic apparatus in the diatom Thalassiosira pseudonana.Plant physiology · 2021Article
- ppGpp influences protein protection, growth and photosynthesis in Phaeodactylum tricornutum.The New phytologist · 2021Article
- Specific Lhc Proteins Are Bound to PSI or PSII Supercomplexes in the DiatomPlant physiology · 2020Article
- Fucoxanthin-Chlorophyll Protein Complexes of the Centric DiatomPlant physiology · 2019Article
- How reduced excitonic coupling enhances light harvesting in the main photosynthetic antennae of diatoms.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diatoms possess fucoxanthin chlorophyll proteins (FCP) as light-harvesting systems. These membrane intrinsic proteins bind fucoxanthin as major carotenoid and Chl c as accessory chlorophyll. The relatively high sequence homology to higher plant light-harvesting complex II gave rise to the assumption of a similar overall structure. From centric diatoms like Cyclotella meneghiniana, however, two major FCP complexes can be isolated. FCPa, composed of Fcp2 and Fcp6 subunits, was demonstrated to be trimeric, whereas FCPb, known to contain Fcp5 polypeptides, is of higher oligomeric state. No molecular structure of either complex is available so far. Here we used electron microscopy and single particle analysis to elucidate the overall architecture of FCPb. The complexes are built from trimers as basic unit, assembling into nonameric moieties. The trimer itself is smaller, i.e. more compact than LHCII, but the main structural features are conserved.
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