ArticlePhotosynthesis research
The PsbP-like protein (sll1418) of Synechocystis sp. PCC 6803 stabilises the donor side of Photosystem II.
Article in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Proximity Labeling Facilitates Defining the Proteome Neighborhood of Photosystem II Oxygen Evolution Complex in a Model Cyanobacterium.Molecular & cellular proteomics : MCP · 2022Article
- Specific Incorporation of Polyunsaturated Fatty Acids into theInternational journal of molecular sciences · 2021Article
- Analysis of a photosynthetic cyanobacterium rich in internal membrane systems via gradient profiling by sequencing (Grad-seq).The Plant cell · 2021Article
- The extrinsic proteins of photosystem II: update.Planta · 2016Review
- Article
- Characterization of a Synechocystis sp. PCC 6803 double mutant lacking the CyanoP and Ycf48 proteins of Photosystem II.Photosynthesis research · 2015Article
- Localization of the CyanoP binding site on photosystem II by surface plasmon resonance spectroscopy.Frontiers in plant science · 2014Article
- The PsbP family of proteins.Photosynthesis research · 2013Review
- Auxiliary proteins involved in the assembly and sustenance of photosystem II.Photosynthesis researchReview
- Article
- Structure, function, and evolution of the PsbP protein family in higher plants.Photosynthesis researchReview
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The PsbP-like protein of the cyanobacterium Synechocystis sp. PCC 6803 is a peripheral component of Photosystem II, located at the lumenal side of the thylakoid membrane. Removal of this protein leads to decreased competitive potential of a PsbP-like deletion mutant when grown in a mixture with wild-type cells. Flash-induced oxygen evolution traces of the mutant show a higher probability of misses, correlated with increased amplitudes of the S-states decay in the dark. Thermoluminescence emission traces demonstrate a changed charge recombination pattern in the mutant, the S(3)Q(B)(-) couple becoming the major species instead of the S(2)Q(B)(-). Our data suggest a possible role of the PsbP-like protein in stabilisation of the charge separation in Photosystem II of cyanobacteria through interaction with the Mn cluster.
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