ArticleThe Journal of biological chemistry2010
Crystal structure of the nitrogenase-like dark operative protochlorophyllide oxidoreductase catalytic complex (ChlN/ChlB)2.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 92 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
- Integrated evaluation of methidathion-induced toxicity in Allium cepa with a multifactorial biological approach.Scientific reports · 2025Article
- Investigation of in-vivo and in-silico toxicity induced by environmental drug contamination in a non-target organism.Scientific reports · 2025Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- Article
- Plastid Genome Evolution of Two Colony-Forming BenthicInternational journal of molecular sciences · 2023Article
- The plastomes ofPlant direct · 2022Article
- An Alternative Proposal for the Reaction Mechanism of Light-Dependent Protochlorophyllide Oxidoreductase.ACS catalysis · 2022Article
- Photocatalysis as the 'master switch' of photomorphogenesis in early plant development.Nature plants · 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
- Special Issue on Nitrogenases and Homologous Systems.Chembiochem : a European journal of chemical biology · 2020Article
- Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
- Anoxygenic Phototrophs Span Geochemical Gradients and Diverse Morphologies in Terrestrial Geothermal Springs.mSystems · 2019Article
- Article
- Evolution of light-independent protochlorophyllide oxidoreductase.Protoplasma · 2019Review
- A physiological perspective on the origin and evolution of photosynthesis.FEMS microbiology reviews · 2018Review
- The Effect of Two Amino acid Residue Substitutions via RNA Editing on Dark-operative Protochlorophyllide Oxidoreductase in the Black Pine Chloroplasts.Scientific reports · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During (bacterio)chlorophyll biosynthesis of many photosynthetically active organisms, dark operative protochlorophyllide oxidoreductase (DPOR) catalyzes the two-electron reduction of ring D of protochlorophyllide to form chlorophyllide. DPOR is composed of the subunits ChlL, ChlN, and ChlB. Homodimeric ChlL(2) bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase transferring single electrons to the heterotetrameric (ChlN/ChlB)(2) complex. The latter contains two intersubunit [4Fe-4S] clusters and two protochlorophyllide binding sites, respectively. Here we present the crystal structure of the catalytic (ChlN/ChlB)(2) complex of DPOR from the cyanobacterium Thermosynechococcus elongatus at a resolution of 2.4 A. Subunits ChlN and ChlB exhibit a related architecture of three subdomains each built around a central, parallel beta-sheet surrounded by alpha-helices. The (ChlN/ChlB)(2) crystal structure reveals a [4Fe-4S] cluster coordinated by an aspartate oxygen alongside three cysteine ligands. Two equivalent substrate binding sites enriched in aromatic residues for protochlorophyllide substrate binding are located at the interface of each ChlN/ChlB half-tetramer. The complete octameric (ChlN/ChlB)(2)(ChlL(2))(2) complex of DPOR was modeled based on the crystal structure and earlier functional studies. The electron transfer pathway via the various redox centers of DPOR to the substrate is proposed.
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