ArticlePloS one2013
Redox-controlled proton gating in bovine cytochrome c oxidase.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 29 citations in OpenAlex.
- The three-dimensional structure of a proton-pumping pathway, the H-pathway, is evolutionarily conserved in all three families of cytochromeFrontiers in chemistry · 2025Article
- Probing the Proton-Loading Site of CytochromeMolecules (Basel, Switzerland) · 2020Article
- Snapshot of an oxygen intermediate in the catalytic reaction of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- Crystal structure of CO-bound cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle.The Journal of biological chemistry · 2016Article
- Proton translocation in cytochrome c oxidase: insights from proton exchange kinetics and vibrational spectroscopy.Biochimica et biophysica acta · 2015Review
- Exceptional longevity and exceptionally high metabolic rates in anthropoid primates are linked to a major modification of the ubiquinone reduction site of cytochrome b.Journal of bioenergetics and biomembranes · 2014Article
- Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin.Journal of the American Chemical Society · 2014Article
- Copper active sites in biology.Chemical reviews · 2014Review
- Direct regulation of cytochrome c oxidase by calcium ions.PloS one · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome c oxidase is the terminal enzyme in the electron transfer chain of essentially all organisms that utilize oxygen to generate energy. It reduces oxygen to water and harnesses the energy to pump protons across the mitochondrial membrane in eukaryotes and the plasma membrane in prokaryotes. The mechanism by which proton pumping is coupled to the oxygen reduction reaction remains unresolved, owing to the difficulty of visualizing proton movement within the massive membrane-associated protein matrix. Here, with a novel hydrogen/deuterium exchange resonance Raman spectroscopy method, we have identified two critical elements of the proton pump: a proton loading site near the propionate groups of heme a, which is capable of transiently storing protons uploaded from the negative-side of the membrane prior to their release into the positive side of the membrane and a conformational gate that controls proton translocation in response to the change in the redox state of heme a. These findings form the basis for a postulated molecular model describing a detailed mechanism by which unidirectional proton translocation is coupled to electron transfer from heme a to heme a 3, associated with the oxygen chemistry occurring in the heme a 3 site, during enzymatic turnover.
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.