ArticlePhotosynthesis research2004
Novel Insights into the Enzymology, Regulation and Physiological Functions of Light-dependent Protochlorophyllide Oxidoreductase in Angiosperms.
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 70 papers.
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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
70 citing papers in PubMed, 176 citations in OpenAlex.
- Turning over a green leaf: integrating light signals toward chloroplast establishment.Plant physiology · 2026Review
- Chloroplastic protein PORC undergoes heat-induced condensation and enhances thermotolerance in Arabidopsis.Plant physiology · 2026Article
- Leaf color variation mechanism of the yellow-to-green mutant 'Breeding science · 2025Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- Light dependent protochlorophyllide oxidoreductase: a succinct look.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Review
- Integrated transcriptomics, metabolomics and physiological analyses reveal differential response mechanisms of wheat to cadmium and/or salinity stress.Frontiers in plant science · 2024Article
- Low-Temperature-Mediated Promoter Methylation Relates to the Expression ofInternational journal of molecular sciences · 2023Article
- Plastid Genome Evolution of Two Colony-Forming BenthicInternational journal of molecular sciences · 2023Article
- Expression ofPlants (Basel, Switzerland) · 2023Article
- Transcriptome Profiling and Chlorophyll Metabolic Pathway Analysis Reveal the Response ofPlants (Basel, Switzerland) · 2023Article
- Article
- Insights into the physiological, molecular, and genetic regulators of albinism inFrontiers in genetics · 2023Article
- How Photoactivation Triggers Protochlorophyllide Reduction: Computational Evidence of a Stepwise Hydride Transfer during Chlorophyll Biosynthesis.ACS catalysis · 2022Article
- An Alternative Proposal for the Reaction Mechanism of Light-Dependent Protochlorophyllide Oxidoreductase.ACS catalysis · 2022Article
- The red/blue light ratios from light-emitting diodes affect growth and flower quality ofFrontiers in plant science · 2022Article
- Plastid and cytoplasmic origins ofFrontiers in plant science · 2022Article
- Chaperone-like protein DAY plays critical roles in photomorphogenesis.Nature communications · 2021Article
- The Role of Tetrapyrrole- and GUN1-Dependent Signaling on Chloroplast Biogenesis.Plants (Basel, Switzerland) · 2021Review
- Mechanism Underlying the Shading-Induced Chlorophyll Accumulation in Tea Leaves.Frontiers in plant science · 2021Article
- Dynamics of Etiolation Monitored by Seedling Morphology, Carotenoid Composition, Antioxidant Level, and Photoactivity of Protochlorophyllide inFrontiers in plant science · 2021Article
10 more citing papers are in PubMed but not listed here.
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
The reduction of protochlorophyllide (Pchlide) is a key regulatory step in the biosynthesis of chlorophyll in phototrophic organisms. Two distinct enzymes catalyze this reduction; a light-dependent NADPH:protochlorophyllide oxidoreductase (POR) and light-independent Pchlide reductase (DPOR). Both enzymes are widely distributed among phototrophic organisms with the exception that only POR is found in angiosperms and only DPOR in anoxygenic photosynthetic bacteria. Consequently, angiosperms become etiolated in the absence of light, since the reduction of Pchlide in angiosperms is solely dependent on POR. In eukaryotic phototrophs, POR is a nuclear-encoded single polypeptide and post-translationally imported into plastids. POR possesses unique features, its light-dependent catalytic activity, accumulation in plastids of dark-grown angiosperms (etioplasts) via binding to its substrate, Pchlide, and cofactor, NADPH, resulting in the formation of prolamellar bodies (PLBs), and rapid degradation after catalysis under subsequent illumination. During the last decade, considerable progress has been made in the study of the gene organization, catalytic mechanism, membrane association, regulation of the gene expression, and physiological function of POR. In this review, we provide a brief overview of DPOR and then summarize the current state of knowledge on the biochemistry and molecular biology of POR mainly in angiosperms. The physiological and evolutional implications of POR are also discussed.
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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.