ArticleThe Journal of biological chemistry2020
Substrate recognition induces sequential electron transfer across subunits in the nitrogenase-like DPOR complex.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 24 citations in OpenAlex.
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 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
- Cross-feeding between cyanobacterium Synechococcus and Escherichia coli in an artificial autotrophic-heterotrophic coculture system revealed by integrated omics analysis.Biotechnology for biofuels and bioproducts · 2022Article
- Chlorophyllides: Preparation, Purification, and Application.Biomolecules · 2021Review
- The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A key step in bacteriochlorophyll biosynthesis is the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide), catalyzed by dark-operative protochlorophyllide oxidoreductase (DPOR). DPOR is made of electron donor (BchL) and acceptor (BchNB) component proteins. BchNB is further composed of two subunits each of BchN and BchB arranged as an α
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.