ArticleCurrent microbiology2008
Redox of plastoquinone pool regulates the expression and activity of NADPH dehydrogenase supercomplex in Synechocystis sp. strain PCC 6803.
Article in Current microbiology, 2008. 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, 17 citations in OpenAlex.
- Microcystin aids in cold temperature acclimation: Differences between a toxic Microcystis wildtype and non-toxic mutant.Harmful algae · 2023Article
- Cool temperature acclimation in toxigenicbioRxiv : the preprint server for biology · 2023Article
- Cyanobacterial NDH-1 Complexes.Frontiers in microbiology · 2022Review
- Plastoquinone and Ubiquinone in Plants: Biosynthesis, Physiological Function and Metabolic Engineering.Frontiers in plant science · 2016Review
- Cyanobacterial phytochrome2 regulates the heterotrophic metabolism and has a function in the heat and high-light stress response.Plant physiology · 2014Article
- Genetic identification of a high-affinity Ni transporter and the transcriptional response to Ni deprivation in Synechococcus sp. strain WH8102.Applied and environmental microbiology · 2012Article
- The interrelationship between the lower oxygen limit, chlorophyll fluorescence and the xanthophyll cycle in plants.Photosynthesis research · 2011Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A highly active NADPH dehydrogenase supercomplex, which is essential for cyclic electron transport around photosystem I (cyclic PSI) and respiration, was newly identified in cyanobacteria. Synechocystis sp. strain PCC 6803 cells were treated with exogenous glucose (Glc) or 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU); subsequently, active staining of NADPH-nitroblue tetrazolium oxidoreductase, western blot, and the initial rate of P700+ dark reduction were assessed in the cyanobacterium at several time points. The expression and enzyme activity levels of NADPH dehydrogenase supercomplex were gradually inhibited and closely associated with the decrease in the rate of cyclic PSI accompanying the addition of exogenous Glc to the cultures. In contrast, the activity levels were significantly stimulated but did not cause an increase in the rate of cyclic PSI as expected in the presence of DCMU. Since Glc results in the partial reduction of the plastoquinone (PQ) pool while DCMU results in the overoxidation of the PQ pool, the present results demonstrate that the expression and activity of NADPH dehydrogenase supercomplex are under the influence of the redox control of the PQ pool while the operation of cyclic PSI as mediated by this supercomplex requires an appropriate redox poise of the PQ pool.
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