ArticlePhotosynthesis research2002
Photosystem I from the unusual cyanobacterium Gloeobacter violaceus.
Article in Photosynthesis research, 2002. 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, 37 citations in OpenAlex.
- Structure and evolution of photosystem I in the early-branching cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Elucidating light-induced changes in excitation energy transfer of photosystem I and II in whole cells of two model cyanobacteria.Photosynthesis research · 2025Article
- Cryo-EM structure of a tetrameric photosystem I fromPlant communications · 2022Article
- Physiological and evolutionary implications of tetrameric photosystem I in cyanobacteria.Nature plants · 2019Article
- Proteomic approaches in research of cyanobacterial photosynthesis.Photosynthesis research · 2015Review
- Characterization and evolution of tetrameric photosystem I from the thermophilic cyanobacterium Chroococcidiopsis sp TS-821.The Plant cell · 2014Article
- Establishment of the reporter system for a thylakoid-lacking cyanobacterium, Gloeobacter violaceus PCC 7421.FEBS open bio · 2013Article
- Properties of photosystem I antenna protein complexes of the diatom Cyclotella meneghiniana.Journal of experimental botany · 2012Article
- The origin of multicellularity in cyanobacteria.BMC evolutionary biology · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosystem I (PS I) from the primitive cyanobacterium Gloeobacter violaceus has been purified and characterised. Despite the fact that the isolated complexes have the same subunit composition as complexes from other cyanobacteria, the amplitude of flash-induced absorption difference spectra indicates a much bigger antenna size with about 150 chlorophylls per P700 as opposed to the usual 90. Image analysis of the PS I preparation from Gloeobacter reveals that the PS I particles exist both in a trimeric and in a monomeric form and that their size and shape closely resembles other cyanobacterial PS I particles. However, the complexes exhibit a higher molecular weight as could be shown by gel filtration. The preparation contains novel polypeptides not related to known Photosystem I subunits. The N-terminal sequence of one of those polypeptides has been determined and reveals no homology to known or hypothetical proteins. Immunoblotting shows a cross-reaction of three of the polypeptide bands with an antibody raised against the major LHC from the diatom Cyclotella cryptica. Electron microscopy reveals a novel T-shaped complex which has never been observed in any other cyanobacterial PS I preparation. 77 K spectra of purified PS I show an extreme blue-shift of the fluorescence emission, indicating an unusual organisation of the PS I antenna system in Gloeobacter.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.