ReviewLife (Basel, Switzerland)2014
Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances.
Review in Life (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 101 citations in OpenAlex.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Electron transport reactions of cyanobacterial photosynthesis and state-of-the-art in vivo measurement techniques.Plant physiology · 2026Review
- Physiological and Transcriptomic Responses ofBiology · 2026Article
- Deciphering the metabolic details of L-lysine toxicity in cyanobacteria.Plant physiology · 2026Article
- Biotechnological Applications of Cyanobacteria: Synechocystis and Synechococcus Strains.Advances in biochemical engineering/biotechnology · 2025Review
- The Feather Moss Hylocomium splendens Affects the Transcriptional Profile of a Symbiotic Cyanobacterium in Relation to Acquisition and Turnover of Key Nutrients.Microbial ecology · 2024Article
- Proteomics analysis reveals differential acclimation of coastal and oceanicFrontiers in microbiology · 2024Article
- Ferredoxin C2 is required for chlorophyll biosynthesis and accumulation of photosynthetic antennae in Arabidopsis.Plant, cell & environment · 2023Article
- A cellular selection identifies elongated flavodoxins that support electron transfer to sulfite reductase.Protein science : a publication of the Protein Society · 2023Article
- Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- Article
- Cyanobacterial Bioenergetics in Relation to Cellular Growth and Productivity.Advances in biochemical engineering/biotechnology · 2023Article
- Photoautotrophic Growth Rate Enhancement ofBiology · 2022Article
- Bioavailable iron titrations reveal oceanic Synechococcus ecotypes optimized for different iron availabilities.ISME communications · 2022Article
- Article
- Spectroscopic and functional characterization of the [2Fe-2S] scaffold protein Nfu from Synechocystis PCC6803.Biochimie · 2022Article
- Exploitation of Hetero- and Phototrophic Metabolic Modules for Redox-Intensive Whole-Cell Biocatalysis.Frontiers in bioengineering and biotechnology · 2022Review
- Diversification of Ferredoxins across Living Organisms.Current issues in molecular biology · 2021Article
- Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria.Plant physiology · 2021Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferredoxins (Fed), occurring in most organisms, are small proteins that use their iron-sulfur cluster to distribute electrons to various metabolic pathways, likely including hydrogen production. Here, we summarize the current knowledge on ferredoxins in cyanobacteria, the prokaryotes regarded as important producers of the oxygenic atmosphere and biomass for the food chain, as well as promising cell factories for biofuel production. Most studies of ferredoxins were performed in the model strain, Synechocystis PCC6803, which possesses nine highly-conserved ferredoxins encoded by monocistronic or operonic genes, some of which are localized in conserved genome regions. Fed1, encoded by a light-inducible gene, is a highly abundant protein essential to photosynthesis. Fed2-Fed9, encoded by genes differently regulated by trophic conditions, are low-abundant proteins that play prominent roles in the tolerance to environmental stresses. Concerning the selectivity/redundancy of ferredoxin, we report that Fed1, Fed7 and Fed9 belong to ferredoxin-glutaredoxin-thioredoxin crosstalk pathways operating in the protection against oxidative and metal stresses. Furthermore, Fed7 specifically interacts with a DnaJ-like protein, an interaction that has been conserved in photosynthetic eukaryotes in the form of a composite protein comprising DnaJ- and Fed7-like domains. Fed9 specifically interacts with the Flv3 flavodiiron protein acting in the photoreduction of O2 to H2O.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.