ArticleThe Journal of biological chemistry2014
NdhO, a subunit of NADPH dehydrogenase, destabilizes medium size complex of the enzyme in Synechocystis sp. strain PCC 6803.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 32 citations in OpenAlex.
- A cyanobacteria-derived intermolecular salt bridge stabilizes photosynthetic NDH-1 and prevents oxidative stress.Communications biology · 2025Article
- Genome-wide insights into the evolutionary history of conserved photosynthetic NDH-1 in cyanobacteria.Frontiers in plant science · 2025Article
- Interplay between photosynthetic electron flux and organic carbon sinks in sucrose-excreting Synechocystis sp. PCC 6803 revealed by omics approaches.Microbial cell factories · 2024Article
- Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations.Communications biology · 2023Article
- NDH-1L with a truncated NdhM subunit is unstable under stress conditions in cyanobacteria.Plant direct · 2023Article
- Screening of mutants using chlorophyll fluorescence.Journal of plant research · 2021Article
- Structural insights into NDH-1 mediated cyclic electron transfer.Nature communications · 2020Article
- Low-Temperature Adaptation of the Snow AlgaFrontiers in microbiology · 2020Article
- Molecular dynamics and structural models of the cyanobacterial NDH-1 complex.Biochimica et biophysica acta. Bioenergetics · 2019Article
- Rational engineering of photosynthetic electron flux enhances light-powered cytochrome P450 activity.Synthetic biology (Oxford, England) · 2018Article
- NDH-1 Is Important for Photosystem I Function ofFrontiers in plant science · 2017Article
- The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria.Plant physiology · 2016Article
- A Cytoplasmic Protein Ssl3829 Is Important for NDH-1 Hydrophilic Arm Assembly in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- Functional Characterization of the Subunits N, H, J, and O of the NAD(P)H Dehydrogenase Complexes in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- NdhM Subunit Is Required for the Stability and the Function of NAD(P)H Dehydrogenase Complexes Involved in CO2 Uptake in Synechocystis sp. Strain PCC 6803.The Journal of biological chemistry · 2016Article
- NdhV Is a Subunit of NADPH Dehydrogenase Essential for Cyclic Electron Transport in Synechocystis sp. Strain PCC 6803.Plant physiology · 2016Article
- Subunit Q Is Required to Stabilize the Large Complex of NADPH Dehydrogenase in Synechocystis sp. Strain PCC 6803.Plant physiology · 2015Article
- A minute-scale P515 kinetic traces light-driven proton gradient formation in dark-incubated Synechocystis sp. PCC 6803.Physiologia plantarumArticle
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two mutants that grew faster than the wild-type (WT) strain under high light conditions were isolated from Synechocystis sp. strain PCC 6803 transformed with a transposon-bearing library. Both mutants had a tag in ssl1690 encoding NdhO. Deletion of ndhO increased the activity of NADPH dehydrogenase (NDH-1)-dependent cyclic electron transport around photosystem I (NDH-CET), while overexpression decreased the activity. Although deletion and overexpression of ndhO did not have significant effects on the amount of other subunits such as NdhH, NdhI, NdhK, and NdhM in the cells, the amount of these subunits in the medium size NDH-1 (NDH-1M) complex was higher in the ndhO-deletion mutant and much lower in the overexpression strain than in the WT. NdhO strongly interacts with NdhI and NdhK but not with other subunits. NdhI interacts with NdhK and the interaction was blocked by NdhO. The blocking may destabilize the NDH-1M complex and repress the NDH-CET activity. When cells were transferred from growth light to high light, the amounts of NdhI and NdhK increased without significant change in the amount of NdhO, thus decreasing the relative amount of NdhO. This might have decreased the blocking, thereby stabilizing the NDH-1M complex and increasing the NDH-CET activity under high light conditions.
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