ArticleNature2010
X-ray crystal structure of the light-independent protochlorophyllide reductase.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 194 citations in OpenAlex.
- De novo coassembly of functional chlorophyll- and carotenoid-protein complexes inScience advances · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Chirality distribution in the fifth ligand coordination of chlorophylls-c in photosynthetic pigment-protein complexes.Photosynthesis research · 2026Article
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Enzyme-Substrate Complex Formation and Electron Transfer in Nitrogenase-Like Dark-Operative Protochlorophyllide Oxidoreductase (DPOR).ChemistryOpen · 2025Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- Nitrogen stable isotope fractionation by biological nitrogen fixation reveals cellular nitrogenase is diffusion limited.PNAS nexus · 2025Article
- Chlorophyll Pigments and Their Synthetic Analogs.Plant & cell physiology · 2025Review
- Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.Nature catalysis · 2025Article
- Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024Review
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- Engineering Chlorophyll, Bacteriochlorophyll, and Carotenoid Biosynthetic Pathways inACS synthetic biology · 2023Article
- Plastid Genome Evolution of Two Colony-Forming BenthicInternational journal of molecular sciences · 2023Article
- Transcriptomic and photosynthetic analyses ofFrontiers in plant science · 2023Article
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- Proton-coupled electron transfer of macrocyclic ring hydrogenation: The chlorinphlorin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Genomic Features of the Bundle-Forming HeliobacteriumMicroorganisms · 2022Article
- Extracellular Vesicle-Mediated Secretion of Protochlorophyllide in the CyanobacteriumPlants (Basel, Switzerland) · 2022Article
- An Alternative Proposal for the Reaction Mechanism of Light-Dependent Protochlorophyllide Oxidoreductase.ACS catalysis · 2022Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthetic organisms adopt two different strategies for the reduction of the C17 = C18 double bond of protochlorophyllide (Pchlide) to form chlorophyllide a, the direct precursor of chlorophyll a (refs 1-4). The first involves the activity of the light-dependent Pchlide oxidoreductase, and the second involves the light-independent (dark-operative) Pchlide oxidoreductase (DPOR). DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer), which are structurally related to nitrogenase Fe protein and MoFe protein, respectively. Here we report the crystal structure of the NB-protein of DPOR from Rhodobacter capsulatus at a resolution of 2.3A. As expected, the overall structure is similar to that of nitrogenase MoFe protein: each catalytic BchN-BchB unit contains one Pchlide and one iron-sulphur cluster (NB-cluster) coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific Pchlide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit. We propose a unique trans-specific reduction mechanism in which the distorted C17-propionate of Pchlide and an aspartate from BchB serve as proton donors for C18 and C17 of Pchlide, respectively. Intriguingly, the spatial arrangement of the NB-cluster and Pchlide is almost identical to that of the P-cluster and FeMo-cofactor in nitrogenase MoFe-protein, illustrating that a common architecture exists to reduce chemically stable multibonds of porphyrin and dinitrogen.
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