ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure and mechanism of a eukaryotic transmembrane ascorbate-dependent oxidoreductase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 74 citations in OpenAlex.
- A multiplant transcriptomic atlas reveals conserved and lineage-specific defense architectures in response toProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Electron currents mediated by tonoplast cytochromes b561.European biophysics journal : EBJ · 2026Review
- Photocatalytic Biohybrid Vesicles.Chemical reviews · 2026Review
- Arabidopsis IONIC CURRENT FAMILY A proteins facilitate environmental calcium acquisition essential for stress tolerance.Nature plants · 2026Article
- Cecytb-2, a CytochromeBiomolecules · 2025Article
- Role of the human cytochrome b561 family in iron metabolism and tumors (Review).Oncology letters · 2025Review
- Article
- Three-Dimensional Interaction Homology: Deconstructing Residue-Residue and Residue-Lipid Interactions in Membrane Proteins.Molecules (Basel, Switzerland) · 2024Article
- Ferric reduction by a CYBDOM protein counteracts increased iron availability in root meristems induced by phosphorus deficiency.Nature communications · 2024Article
- Cellular production of a de novo membrane cytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Spectral and Redox Properties of a Recombinant Mouse CytochromeMolecules (Basel, Switzerland) · 2023Article
- Novel genetically encoded tools for imaging or silencing neuropeptide release from presynaptic terminalsbioRxiv : the preprint server for biology · 2023Article
- Comparison of insect and human cytochrome b561 proteins: Insights into candidate ferric reductases in insects.PloS one · 2023Article
- Distribution and diversity of ROS-generating enzymes across the animal kingdom, with a focus on sponges (Porifera).BMC biology · 2022Article
- Article
- Manipulating the position of DNA expression cassettes using location tags fused to dCas9 (Cas9-Lag) to improve metabolic pathway efficiency.Microbial cell factories · 2020Article
- Structures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.Nature structural & molecular biology · 2020Article
- Expansion of the Major Facilitator Superfamily (MFS) to include novel transporters as well as transmembrane-acting enzymes.Biochimica et biophysica acta. Biomembranes · 2020Article
- Visualizing the protons in a metalloenzyme electron proton transfer pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Direct measurements of ferric reductase activity of human 101F6 and its enhancement upon reconstitution into phospholipid bilayer nanodisc.Biochemistry and biophysics reports · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vitamin C, also known as ascorbate, is required in numerous essential metabolic reactions in eukaryotes. The eukaryotic ascorbate-dependent oxidoreductase cytochrome b561 (Cyt b561), a family of highly conserved transmembrane enzymes, plays an important role in ascorbate recycling and iron absorption. Although Cyt b561 was identified four decades ago, its atomic structure and functional mechanism remain largely unknown. Here, we report the high-resolution crystal structures of cytochrome b561 from Arabidopsis thaliana in both substrate-free and substrate-bound states. Cyt b561 forms a homodimer, with each protomer consisting of six transmembrane helices and two heme groups. The negatively charged substrate ascorbate, or monodehydroascorbate, is enclosed in a positively charged pocket on either side of the membrane. Two highly conserved amino acids, Lys(81) and His(106), play an essential role in substrate recognition and catalysis. Our structural and biochemical analyses allow the proposition of a general electron transfer mechanism for members of the Cyt b561 family.
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.