ArticleThe Journal of biological chemistry2015
Plant Protochlorophyllide Oxidoreductases A and B: CATALYTIC EFFICIENCY AND INITIAL REACTION STEPS.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 43 citations in OpenAlex.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Multi-omics analysis reveals the crucial role of ligustrum lucidum carbon dots in promoting vegetable sweetpotato growth and enhancing soil health.BMC plant biology · 2026Article
- Interpretable multi-omics machine learning reveals drought-driven shifts in plant-microbe interactions.Environmental microbiome · 2026Article
- Discovery of a MarineMarine drugs · 2026Article
- Light dependent protochlorophyllide oxidoreductase: a succinct look.Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Review
- Genome-wide association of dry (Tamar) date palm fruit color.The plant genome · 2023Article
- Phosphorus Acquisition Efficiency and Transcriptomic Changes in Maize Plants Treated with Two Lignohumates.Plants (Basel, Switzerland) · 2023Article
- A Label-Free Proteomic and Complementary Metabolomic Analysis of Leaves of the Resurrection PlantLife (Basel, Switzerland) · 2021Article
- Chlorophyllides: Preparation, Purification, and Application.Biomolecules · 2021Review
- New insights into the response of maize to fluctuations in the light environment.Molecular genetics and genomics : MGG · 2021Article
- Photocatalysis as the 'master switch' of photomorphogenesis in early plant development.Nature plants · 2021Review
- The Role of Membranes and Lipid-Protein Interactions in the Mg-Branch of Tetrapyrrole Biosynthesis.Frontiers in plant science · 2021Review
- Mechanism Underlying the Shading-Induced Chlorophyll Accumulation in Tea Leaves.Frontiers in plant science · 2021Article
- Article
- Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Zucchini Plants Alter Gene Expression and Emission of (Frontiers in plant science · 2020Article
- NADPH:protochlorophyllide oxidoreductase B (PORB) action in Arabidopsis thaliana revisited through transgenic expression of engineered barley PORB mutant proteins.Plant molecular biology · 2017Article
- Transcriptional and post-translational control of chlorophyll biosynthesis by dark-operative protochlorophyllide oxidoreductase in Norway spruce.Photosynthesis research · 2017Article
- Vertebrate Cryptochromes are Vestigial Flavoproteins.Scientific reports · 2017Article
- Multiple active site residues are important for photochemical efficiency in the light-activated enzyme protochlorophyllide oxidoreductase (POR).Journal of photochemistry and photobiology. B, Biology · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzyme protochlorophyllide oxidoreductase (POR, EC 1.3.1.33) has a key role in plant development. It catalyzes one of the later steps in chlorophyll synthesis, the light-induced reduction of protochlorophyllide (PChlide) into chlorophyllide (Chlide) in the presence of NADPH. Two isozymes of plant POR, POR A and POR B from barley, which differ in their function during plant life, are compared with respect to their substrate binding affinity, catalytic efficiency, and catalytic mechanism. POR B as compared with POR A shows an 5-fold higher binding affinity for PChlide and an about 6-fold higher catalytic efficiency measured as kcat/Km. Based on the reaction intermediates, which can be trapped at low temperatures the same reaction mechanism operates in both POR A and POR B. In contrast to results reported for POR enzymes from cyanobacteria, the initial light-driven step, which occurs at temperatures below 180 K already involves the full chemistry of the photoreduction and yields the reaction product, Chlide, in an enzyme-bound form. The subsequent dark reactions, which include cofactor (NADP(+)) release and cofactor (NADPH) rebinding, show different temperature dependences for POR A and POR B and suggest a higher conformational flexibility of POR B in the surrounding active center. Both the higher substrate binding affinity and well adapted enzyme dynamics are held responsible for the increased catalytic activity of POR B as compared with POR A.
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