ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 68 citations in OpenAlex.
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.Nature catalysis · 2025Article
- Improving macromolecular structure refinement with metal-coordination restraints.Acta crystallographica. Section D, Structural biology · 2024Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Structural basis for coupled ATP-driven electron transfer in the double-cubane cluster protein.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Extracellular Vesicle-Mediated Secretion of Protochlorophyllide in the CyanobacteriumPlants (Basel, Switzerland) · 2022Article
- Occurrence, Evolution and Specificities of Iron-Sulfur Proteins and Maturation Factors in Chloroplasts from Algae.International journal of molecular sciences · 2021Review
- Substrate recognition induces sequential electron transfer across subunits in the nitrogenase-like DPOR complex.The Journal of biological chemistry · 2020Article
- Chimeric Interaction of Nitrogenase-Like Reductases with the MoFe Protein of Nitrogenase.Chembiochem : a European journal of chemical biology · 2020Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Elevated Expression of a Functional Suf Pathway in Escherichia coli BL21(DE3) Enhances Recombinant Production of an Iron-Sulfur Cluster-Containing Protein.Journal of bacteriology · 2020Article
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.Nucleic acids research · 2019Article
- Evolution of light-independent protochlorophyllide oxidoreductase.Protoplasma · 2019Review
- Sequential and differential interaction of assembly factors during nitrogenase MoFe protein maturation.The Journal of biological chemistry · 2018Article
- ATP-dependent substrate reduction at an [FeProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Effect of Two Amino acid Residue Substitutions via RNA Editing on Dark-operative Protochlorophyllide Oxidoreductase in the Black Pine Chloroplasts.Scientific reports · 2017Article
- Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthesis uses chlorophylls for the conversion of light into chemical energy, the driving force of life on Earth. During chlorophyll biosynthesis in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase (DPOR), a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-electron reduction of the fully conjugated ring system of protochlorophyllide a. The reduction of the C-17=C-18 double bond results in the characteristic ring architecture of all chlorophylls, thereby altering the absorption properties of the molecule and providing the basis for light-capturing and energy-transduction processes of photosynthesis. We report the X-ray crystallographic structure of the substrate-bound, ADP-aluminium fluoride-stabilized (ADP·AlF(3)-stabilized) transition state complex between the DPOR components L(2) and (NB)(2) from the marine cyanobacterium Prochlorococcus marinus. Our analysis permits a thorough investigation of the dynamic interplay between L(2) and (NB)(2). Upon complex formation, substantial ATP-dependent conformational rearrangements of L(2) trigger the protein-protein interactions with (NB)(2) as well as the electron transduction via redox-active [4Fe-4S] clusters. We also present the identification of artificial "small-molecule substrates" of DPOR in correlation with those of nitrogenase. The catalytic differences and similarities between DPOR and nitrogenase have broad implications for the energy transduction mechanism of related multiprotein complexes that are involved in the reduction of chemically stable double and/or triple bonds.
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