ArticlePlant physiology2006
Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana.
Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed, 105 citations in OpenAlex.
- Genome analysis of dark-adapted variants identifies the phosphatase gene phsP involved in the regulation of photosynthetic and dark-heterotrophic growth in the cyanobacterium Leptolyngbya boryana.Plant & cell physiology · 2025Article
- Simultaneous acclimation to nitrogen and iron scarcity in open ocean cyanobacteria revealed by sparse tensor decomposition of metatranscriptomes.Science advances · 2025Article
- Extracellular Vesicle-Mediated Secretion of Chlorophyll Biosynthetic Intermediates in the Cyanobacterium Leptolyngbya boryana.Plant & cell physiology · 2025Article
- Enhancing photosynthetic efficiency in Phalaenopsis amabilis through bioreactor innovations.BMC plant biology · 2024Article
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- Heterotrophy Compared to Photoautotrophy for Growth Characteristics and Pigment Compositions in Batch Cultures of Four Green Microalgae.Plants (Basel, Switzerland) · 2024Article
- Genome-wide association of dry (Tamar) date palm fruit color.The plant genome · 2023Article
- Absolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803.Photosynthesis research · 2023Article
- Effects of Light and Oxygen on Chlorophyll d Biosynthesis in a Marine Cyanobacterium Acaryochloris marinaPlants (Basel, Switzerland) · 2022Article
- Extracellular Vesicle-Mediated Secretion of Protochlorophyllide in the CyanobacteriumPlants (Basel, Switzerland) · 2022Article
- Nanoscale zero-valent iron alters physiological, biochemical, and transcriptomic response of nonylphenol-exposed algae (Dictyosphaerium sp.).Environmental science and pollution research international · 2022Article
- Complex Evolution of Light-Dependent Protochlorophyllide Oxidoreductases in Aerobic Anoxygenic Phototrophs: Origin, Phylogeny, and Function.Molecular biology and evolution · 2021Article
- The Role of Membranes and Lipid-Protein Interactions in the Mg-Branch of Tetrapyrrole Biosynthesis.Frontiers in plant science · 2021Review
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- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Deep-sea corals provide new insight into the ecology, evolution, and the role of plastids in widespread apicomplexan symbionts of anthozoans.Microbiome · 2020Article
- Anoxygenic Phototrophs Span Geochemical Gradients and Diverse Morphologies in Terrestrial Geothermal Springs.mSystems · 2019Article
- A Photosynthesis-Specific Rubredoxin-Like Protein Is Required for Efficient Association of the D1 and D2 Proteins during the Initial Steps of Photosystem II Assembly.The Plant cell · 2019Article
- Article
- Evolution of light-independent protochlorophyllide oxidoreductase.Protoplasma · 2019Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most oxygenic phototrophs, including cyanobacteria, have two structurally unrelated protochlorophyllide (Pchlide) reductases in the penultimate step of chlorophyll biosynthesis. One is light-dependent Pchlide reductase (LPOR) and the other is dark-operative Pchlide reductase (DPOR), a nitrogenase-like enzyme assumed to be sensitive to oxygen. Very few studies have been conducted on how oxygen-sensitive DPOR operates in oxygenic phototrophic cells. Here, we report that anaerobic conditions are required for DPOR to compensate for the loss of LPOR in cyanobacterial cells. An LPOR-lacking mutant of the cyanobacterium Leptolyngbya boryana (formerly Plectonema boryanum) failed to grow in high light conditions and this phenotype was overcome by cultivating it under anaerobic conditions (2% CO(2)/N(2)). The critical oxygen level enabling the mutant to grow in high light was determined to be 3% (v/v). Oxygen-sensitive Pchlide reduction activity was successfully detected as DPOR activity in cell-free extracts of anaerobically grown mutants, whereas activity was undetectable in the wild type. The content of two DPOR subunits, ChlL and ChlN, was significantly increased in mutant cells compared with wild type. This suggests that the increase in subunits stimulates the DPOR activity that is protected efficiently from oxygen by anaerobic environments, resulting in complementation of the loss of LPOR. These results provide important concepts for understanding how dual Pchlide reductases operate differentially in oxygenic photosynthetic cells grown under natural environments where oxygen levels undergo dynamic changes. The evolutionary implications of the coexistence of two Pchlide reductases are discussed.
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