ArticlePhotosynthesis research2004
Structural Basis of Redox Signaling in Photosynthesis: Structure and Function of Ferredoxin:thioredoxin Reductase and Target Enzymes.
Article in Photosynthesis research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 51 citations in OpenAlex.
- Physiological responses and proteomic analysis of different barley varieties under alkaline stress.Scientific reports · 2026Article
- Divergent Protein Redox Dynamics and Their Relationship with Electron Transport Efficiency during Photosynthesis Induction.Plant & cell physiology · 2024Article
- Comparative transcriptomic and proteomic analyses of two salt-tolerant alfalfa (Frontiers in plant science · 2024Article
- The Assembly of Super-Complexes in the Plant Chloroplast.Biomolecules · 2021Review
- Photosynthetic Phosphoribulokinase Structures: Enzymatic Mechanisms and the Redox Regulation of the Calvin-Benson-Bassham Cycle.The Plant cell · 2020Article
- New Light on Chloroplast Redox Regulation: Molecular Mechanism of Protein Thiol Oxidation.Frontiers in plant science · 2019Review
- Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.Molecular & cellular proteomics : MCP · 2014Article
- Redox regulation of the Calvin-Benson cycle: something old, something new.Frontiers in plant science · 2013Review
- Peroxiredoxins and NADPH-dependent thioredoxin systems in the model legume Lotus japonicus.Plant physiology · 2011Article
- The chloroplastic thiol reducing systems: dual functions in the regulation of carbohydrate metabolism and regeneration of antioxidant enzymes, emphasis on the poplar redoxin equipment.Photosynthesis research · 2010Review
- Chloroplast NADPH-thioredoxin reductase interacts with photoperiodic development in Arabidopsis.Plant physiology · 2009Article
- Role of histidine-86 in the catalytic mechanism of ferredoxin:thioredoxin reductase.Biochemistry · 2009Article
- Sequence and expression analysis of the thioredoxin protein gene family in rice.Molecular genetics and genomics : MGG · 2008Article
- Thioredoxins in chloroplasts.Current genetics · 2007Review
- Reconstitution and properties of the recombinant glyceraldehyde-3-phosphate dehydrogenase/CP12/phosphoribulokinase supramolecular complex of Arabidopsis.Plant physiology · 2005Article
- Dynamics of fluxes through photosynthetic complexes in response to changing light and inorganic carbon acclimation in Synechococcus elongatus.Photosynthesis research · 2005Article
- Ferredoxin:thioredoxin Reductase: Disulfide Reduction Catalyzed via Novel Site-specific [4Fe-4S] Cluster Chemistry.Photosynthesis research · 2004Article
Corrections and comments
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Authors and funding
5 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The role of the ferredoxin:thioredoxin system in the reversible light activation of chloroplast enzymes by thiol-disulfide interchange with thioredoxins is now well established. Recent fruitful collaboration between biochemists and structural biologists, reflected by the shared authorship of the paper, allowed to solve the structures of all of the components of the system, including several target enzymes, thus providing a structural basis for the elucidation of the activation mechanism at a molecular level. In the present Review, these structural data are analyzed in conjunction with the information that was obtained previously through biochemical and site-directed mutagenesis approaches. The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms. Thioredoxins in turn reduce regulatory disulfides of various target enzymes. This process triggers conformational changes on these enzymes, allowing them to reach optimal activity. No common activation mechanism can be put forward for these enzymes, as every thioredoxin-regulated protein undergoes specific structural modifications. It is thus important to solve the structures of the individual target enzymes in order to fully understand the molecular mechanism of the redox regulation of each of them.
Identifiers
What OpenQuestion holds
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.