ArticlePhotosynthesis research
Spectral properties of the CP43-deletion mutant of Synechocystis sp. PCC 6803.
Article in Photosynthesis research. 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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7 citing papers in PubMed, 16 citations in OpenAlex.
- Changes in light-harvesting and energy-transfer processes of the chlorophyll d-dominated cyanobacterium Acaryochloris marina in response to different light qualities.Photosynthesis research · 2025Article
- Feeding the world: improving photosynthetic efficiency for sustainable crop production.Journal of experimental botany · 2019Review
- Variety in excitation energy transfer processes from phycobilisomes to photosystems I and II.Photosynthesis research · 2017Article
- Mass spectrometry-based cross-linking study shows that the Psb28 protein binds to cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Heat-induced unfolding of apo-CP43 studied by fluorescence spectroscopy and CD spectroscopy.Photosynthesis research · 2015Article
- Subunit composition of CP43-less photosystem II complexes of Synechocystis sp. PCC 6803: implications for the assembly and repair of photosystem II.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Article
- Recent advances in understanding the assembly and repair of photosystem II.Annals of botany · 2010Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spectral properties, particularly fluorescence spectra and their time-dependent behavior, were investigated for a mutant of the cyanobacterium Synechocystis sp. PCC 6803 lacking the 43 kDa chlorophyll-protein (CP43, PsbC). Lack of CP43 was confirmed by a size shift of the corresponding gene and by Western blotting. The CP43-deletion mutant grown under heterotrophic conditions accumulated a small amount of photosystem (PS) II, but virtually no PS II fluorescence was observed. A 686-nm fluorescence band was clearly observed by phycocyanin excitation, coming from the terminal pigments of phycobilisomes. In contrast, no PS I fluorescence was detected by phycocyanin excitation when accumulation of PS II components was not proved by a fluorescence excitation spectrum, indicating that energy transfer to PS I chlorophyll a was mediated by PS II chlorophyll a. Direct connection of phycobilisomes with PS I was not suggested. Based on these fluorescence properties, the energy flow in the CP43-deletion mutant cells is discussed.
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