ArticleScience (New York, N.Y.)2010
An electronic bus bar lies in the core of cytochrome bc1.
Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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
55 citing papers in PubMed.
- Distinct ubiquinone binding at the oxidation and reduction sites of cytochrome bcProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.Protein science : a publication of the Protein Society · 2024Article
- Long-range charge transfer mechanism of the IIINature communications · 2024Article
- Analysis of lettuce transcriptome reveals the mechanism of different light/dark cycle in promoting the growth and quality.Frontiers in plant science · 2024Article
- Cryo-EM structure of the four-subunitProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structures of the CcmABCD heme release complex at multiple states.Nature communications · 2022Article
- Article
- Cryo-EM structures of the Synechocystis sp. PCC 6803 cytochrome b6f complex with and without the regulatory PetP subunit.The Biochemical journal · 2022Article
- Structures ofScience (New York, N.Y.) · 2022Article
- Quinone binding sites of cyt bc complexes analysed by X-ray crystallography and cryogenic electron microscopy.Biochemical Society transactions · 2022Review
- Structural basis for safe and efficient energy conversion in a respiratory supercomplex.Nature communications · 2022Article
- Sex-specific genetic regulation of adipose mitochondria and metabolic syndrome by Ndufv2.Nature metabolism · 2021Article
- Catalytic Reactions and Energy Conservation in the CytochromeChemical reviews · 2021Review
- Cryo-EM structures of engineered active bcNature communications · 2021Article
- Mechanisms of Mitochondrial ROS Production in Assisted Reproduction: The Known, the Unknown, and the Intriguing.Antioxidants (Basel, Switzerland) · 2020Review
- Universal free-energy landscape produces efficient and reversible electron bifurcation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A spontaneous mitonuclear epistasis converging on Rieske Fe-S protein exacerbates complex III deficiency in mice.Nature communications · 2020Article
- Cryo-EM structure of the spinach cytochrome bNature · 2019Article
- The dependence of brain mitochondria reactive oxygen species production on oxygen level is linear, except when inhibited by antimycin A.Journal of neurochemistry · 2019Article
- Redox-Driven Proton Pumps of the Respiratory Chain.Biophysical journal · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The ubiquinol-cytochrome c oxidoreductases, central to cellular respiration and photosynthesis, are homodimers. High symmetry has frustrated resolution of whether cross-dimer interactions are functionally important. This has resulted in a proliferation of contradictory models. Here, we duplicated and fused cytochrome b subunits, and then broke symmetry by introducing independent mutations into each monomer. Electrons moved freely within and between monomers, crossing an electron-transfer bridge between two hemes in the core of the dimer. This revealed an H-shaped electron-transfer system that distributes electrons between four quinone oxidation-reduction terminals at the corners of the dimer within the millisecond time scale of enzymatic turnover. Free and unregulated distribution of electrons acts like a molecular-scale bus bar, a design often exploited in electronics.
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.