ArticleBiochemistry2015
Complete topology of the RNF complex from Vibrio cholerae.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 36 citations in OpenAlex.
- Evolution and diversity of oxidoreductases involved in redox balance and energy conservation.Nature ecology & evolution · 2026Article
- Identification of key steps in the evolution of anaerobic methanotrophy inScience advances · 2025Article
- Functional Characterization of RseC in the SoxR Reducing System and Its Role in Oxidative Stress Response inJournal of microbiology and biotechnology · 2024Article
- Article
- Metatranscriptomic insights into the microbial electrosynthesis of acetate by FeWorld journal of microbiology & biotechnology · 2023Article
- Purification and structural characterization of the NaNature communications · 2022Article
- Article
- Clostridium sporogenes uses reductive Stickland metabolism in the gut to generate ATP and produce circulating metabolites.Nature microbiology · 2022Article
- Characterization of components of a reducing system for SoxR in the cytoplasmic membrane of Escherichia coli.Journal of microbiology (Seoul, Korea) · 2022Article
- The Rnf complex is a NaCommunications biology · 2020Article
- Seawater salt-trapped Pseudomonas aeruginosa survives for years and gets primed for salinity tolerance.BMC microbiology · 2019Article
- The Rnf Complex Is an Energy-Coupled Transhydrogenase Essential To Reversibly Link Cellular NADH and Ferredoxin Pools in the Acetogen Acetobacterium woodii.Journal of bacteriology · 2018Article
- Transcriptional Analysis of an Ammonium-Excreting Strain of Azotobacter vinelandii Deregulated for Nitrogen Fixation.Applied and environmental microbiology · 2017Article
- Acetate Metabolism in Anaerobes from the Domain Archaea.Life (Basel, Switzerland) · 2015Review
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 1 institution in 1 country.
Funding
Abstract
RNF is a redox-driven ion (Na(+) and in one case possibly H(+)) transporter present in many prokaryotes. It has been proposed that RNF performs a variety of reactions in different organisms, delivering low-potential reducing equivalents for specific cellular processes. RNF shares strong homology with the Na(+)-pumping respiratory enzyme Na(+)-NQR, although there are significant differences in subunit and redox cofactor composition. Here we report a topological analysis of the six subunits of RNF from Vibrio cholerae. Although individual subunits from other organisms have previously been studied, this is the first complete, experimentally derived, analysis of RNF from any one source. This has allowed us to identify and confirm key properties of RNF. The putative NADH binding site in RnfC is located on the cytoplasmic side of the membrane. FeS centers in RnfB and RnfC are also located on the cytoplasmic side. However, covalently attached FMNs in RnfD and RnfG are both located in the periplasm. RNF also contains a number of acidic residues that correspond to functionally important groups in Na(+)-NQR. The acidic residues involved in Na(+) uptake and many of those implicated in Na(+) translocation are topologically conserved. The topology of RNF closely matches the topology represented in the newly published structure of Na(+)-NQR, consistent with the close relation between the two enzymes. The topology of RNF is discussed in the context of the current structural model of Na(+)-NQR, and the proposed functionality of the RNF complex itself.
Indexed as
Identifiers
What OpenQuestion holds
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.