ArticlePhotosynthesis research2015
NDH-1L interacts with ferredoxin via the subunit NdhS in Thermosynechococcus elongatus.
Article in Photosynthesis research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Mechanisms for Generating Low Potential Electrons across the Metabolic Diversity of Nitrogen-Fixing Bacteria.Applied and environmental microbiology · 2023Review
- Cyanobacterial NDH-1 Complexes.Frontiers in microbiology · 2022Review
- Trimeric organization of photosystem I is required to maintain the balanced photosynthetic electron flow in cyanobacterium Synechocystis sp. PCC 6803.Photosynthesis research · 2020Article
- Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase.Nature communications · 2020Article
- Metalloproteins in the Biology of Heterocysts.Life (Basel, Switzerland) · 2019Review
- Molecular dynamics and structural models of the cyanobacterial NDH-1 complex.Biochimica et biophysica acta. Bioenergetics · 2019Article
- Article
- Heterocyst Thylakoid Bioenergetics.Life (Basel, Switzerland) · 2019Review
- Mechanisms of carbon dioxide acquisition and COPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- The NDH-1L-PSI Supercomplex Is Important for Efficient Cyclic Electron Transport in Cyanobacteria.Plant physiology · 2016Article
- NdhV subunit regulates the activity of type-1 NAD(P)H dehydrogenase under high light conditions in cyanobacterium Synechocystis sp. PCC 6803.Scientific reports · 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
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The large size complex of cyanobacterial NAD(P)H dehydrogenase (NDH-1) complex (NDH-1L) plays crucial role in a variety of bioenergetic reactions such as respiration and cyclic electron flow around photosystem I. Although the complex has been isolated and identified, its biochemical function still remains to be clarified. Here, we highly purified the NDH-1L complex from the cells of Thermosynechococcus elongatus by Ni(2+) affinity chromatography and size-exclusion chromatography. The purified NDH-1L complex has an apparent total molecular mass of approximately 500 kDa. 14 known subunits were identified by mass spectrometry and immunoblotting, including the NdhS subunit containing ferredoxin (Fd)-docking site domain. Surface plasmon resonance measurement demonstrates that the NDH-1L complex could bind to Fd with the binding constant (K D) of 59 µM. Yeast two-hybrid system assay further confirmed the interaction of Fd with NdhS and indicated that NdhH is involved in the interaction. Our results provide direct biochemical evidence that the cyanobacterial NDH-1 complex catalyzes the electron transport from reduced Fd to plastoquinone via NdhS and NdhH.
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