ArticleProceedings of the National Academy of Sciences of the United States of America2006
A second isoform of the ferredoxin:NADP oxidoreductase generated by an in-frame initiation of translation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Advances in Decoding Bacterial N-Terminal Proteoforms: Technologies, Challenges, and Functional Insights.Microorganisms · 2026Review
- Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026Article
- Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2026Article
- EPR studies of ferredoxin in spinach and cyanobacterial thylakoids related to photosystem I-driven NADPPhotosynthesis research · 2024Article
- Antenna Modification in a Fast-Growing Cyanobacterium Synechococcus elongatus UTEX 2973 Leads to Improved Efficiency and Carbon-Neutral Productivity.Microbiology spectrum · 2023Article
- Mechanisms for Generating Low Potential Electrons across the Metabolic Diversity of Nitrogen-Fixing Bacteria.Applied and environmental microbiology · 2023Review
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- Attachment of Ferredoxin: NADPMicroorganisms · 2022Article
- Order-of-magnitude enhancement in photocurrent generation of Synechocystis sp. PCC 6803 by outer membrane deprivation.Nature communications · 2022Article
- Cyclic Electron Flow-Coupled Proton Pumping inMicroorganisms · 2022Article
- Introduction of NADH-dependent nitrate assimilation in Synechococcus sp. PCC 7002 improves photosynthetic production of 2-methyl-1-butanol and isobutanol.Metabolic engineering · 2022Article
- Tandem gene amplification restores photosystem II accumulation in cytochrome bThe New phytologist · 2022Article
- Depletion of m-type thioredoxin impairs photosynthesis, carbon fixation, and oxidative stress in cyanobacteria.Plant physiology · 2021Article
- Structure of cyanobacterial phycobilisome core revealed by structural modeling and chemical cross-linking.Science advances · 2021Article
- Phycobilisomes Harbor FNRmBio · 2019Article
- Genes within Genes in Bacterial Genomes.Microbiology spectrum · 2018Review
- Structural integrity of Synechocystis sp. PCC 6803 phycobilisomes evaluated by means of differential scanning calorimetry.Photosynthesis research · 2018Article
- Molecular and functional characterization of ferredoxin NADP(H) oxidoreductase from Gracilaria chilensis and its complex with ferredoxin.Biological research · 2017Article
- Interaction and electron transfer between ferredoxin-NADPPhotosynthesis research · 2017Review
- Evolution of the acceptor side of photosystem I: ferredoxin, flavodoxin, and ferredoxin-NADPPhotosynthesis research · 2017Review
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4 authors.
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Abstract
Ferredoxin:NADP oxidoreductases (FNRs) constitute a family of flavoenzymes that catalyze the exchange of reducing equivalents between one-electron carriers and the two-electron-carrying NADP(H). The main role of FNRs in cyanobacteria and leaf plastids is to provide the NADPH for photoautotrophic metabolism. In root plastids, a distinct FNR isoform is found that has been postulated to function in the opposite direction, providing electrons for nitrogen assimilation at the expense of NADPH generated by heterotrophic metabolism. A multiple gene family encodes FNR isoenzymes in plants, whereas there is only one FNR gene (petH) in cyanobacteria. Nevertheless, we detected two FNR isoforms in the cyanobacterium Synechocystis sp. strain PCC6803. One of them (FNR(S) approximately 34 kDa) is similar in size to the plastid FNR and specifically accumulates under heterotrophic conditions, whereas the other one (FNR(L) approximately 46 kDa) contains an extra N-terminal domain that allows its association with the phycobilisome. Site-directed mutants allowed us to conclude that the smaller isoform, FNR(S), is produced from an internal ribosome entry site within the petH ORF. Thus we have uncovered a mechanism by which two isoforms are produced from a single gene, which is, to our knowledge, novel in photosynthetic bacteria. Our results strongly suggest that FNR(L) is an NADP(+) reductase, whereas FNR(S) is an NADPH oxidase.
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