ArticleProceedings of the National Academy of Sciences of the United States of America2008
Glutamic acid 242 is a valve in the proton pump of cytochrome c oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 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
62 citing papers in PubMed, 136 citations in OpenAlex.
- Molecular and energetic basis of histidine switch dynamics in respiratory complex I.Protein science : a publication of the Protein Society · 2026Article
- Molecular Principles of Gating Proton Transport in the Antiporter Modules of Respiratory Complex I.Journal of the American Chemical Society · 2026Article
- Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductaseProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Current Flow in Nerves and Mitochondria: An Electro-Osmotic Approach.Biomolecules · 2025Review
- Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025Review
- Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2024Article
- Long-range charge transfer mechanism of the IIINature communications · 2024Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Electric fields control water-gated proton transfer in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis for safe and efficient energy conversion in a respiratory supercomplex.Nature communications · 2022Article
- Functional Dynamics of an Ancient Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2021Article
- Architecture of bacterial respiratory chains.Nature reviews. Microbiology · 2021Review
- Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2021Article
- Electron Transfer Coupled to Conformational Dynamics in Cell Respiration.Frontiers in molecular biosciences · 2021Article
- Quantification of Local Electric Field Changes at the Active Site of CytochromeFrontiers in chemistry · 2021Article
- The Redox-Active Tyrosine Is Essential for Proton Pumping in Cytochrome c Oxidase.Frontiers in chemistry · 2021Article
- Snapshot of an oxygen intermediate in the catalytic reaction of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mechanism of proton transfer through the KBiochimica et biophysica acta. Bioenergetics · 2018Article
- Redox-Driven Proton Pumps of the Respiratory Chain.Biophysical journal · 2018Article
- Dewetting transitions coupled to K-channel activation in cytochromeChemical science · 2018Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Aerobic life is based on a molecular machinery that utilizes oxygen as a terminal electron sink. The membrane-bound cytochrome c oxidase (CcO) catalyzes the reduction of oxygen to water in mitochondria and many bacteria. The energy released in this reaction is conserved by pumping protons across the mitochondrial or bacterial membrane, creating an electrochemical proton gradient that drives production of ATP. A crucial question is how the protons pumped by CcO are prevented from flowing backwards during the process. Here, we show by molecular dynamics simulations that the conserved glutamic acid 242 near the active site of CcO undergoes a protonation state-dependent conformational change, which provides a valve in the pumping mechanism. The valve ensures that at any point in time, the proton pathway across the membrane is effectively discontinuous, thereby preventing thermodynamically favorable proton back-leakage while maintaining an overall high efficiency of proton translocation. Suppression of proton leakage is particularly important in mitochondria under physiological conditions, where production of ATP takes place in the presence of a high electrochemical proton gradient.
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.