ArticleProceedings of the National Academy of Sciences of the United States of America2014
Characterizing the proton loading site in cytochrome c oxidase.
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 25 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
25 citing papers in PubMed, 65 citations in OpenAlex.
- Spectroscopic elucidation of an electron-delocalized copper-tyrosine state in heme-copper oxidases reveals its role in proton pumping.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Quinones operate as proton-collecting antennas in energy-transducing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Proton Transfer through a Charged Conduit in Respiratory Complex I: Long-Range Effects and Conformational Gating.Journal of chemical information and modeling · 2025Article
- Structural and functional mechanisms of cytochrome c oxidase.Journal of inorganic biochemistry · 2025Review
- Long-range charge transfer mechanism of the IIINature communications · 2024Article
- Structural insights into functional properties of the oxidized form of cytochrome c oxidase.Nature communications · 2023Article
- Article
- 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
- The three-spin intermediate at the O-O cleavage and proton-pumping junction in heme-Cu oxidases.Science (New York, N.Y.) · 2021Article
- Article
- Probing the Proton-Loading Site of CytochromeMolecules (Basel, Switzerland) · 2020Article
- 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
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- Cavity hydration dynamics in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.Scientific reports · 2017Article
- ns-μs Time-Resolved Step-Scan FTIR of ba₃ Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927.International journal of molecular sciences · 2016Article
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.The Journal of biological chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome c oxidase (CcO) uses the energy released by reduction of O2 to H2O to drive eight charges from the high pH to low pH side of the membrane, increasing the electrochemical gradient. Four electrons and protons are used for chemistry, while four more protons are pumped. Proton pumping requires that residues on a pathway change proton affinity through the reaction cycle to load and then release protons. The protonation states of all residues in CcO are determined in MultiConformational Continuum Electrostatics simulations with the protonation and redox states of heme a, a3, Cu(B), Y288, and E286 used to define the catalytic cycle. One proton is found to be loaded and released from residues identified as the proton loading site (PLS) on the P-side of the protein in each of the four CcO redox states. Thus, the same proton pumping mechanism can be used each time CcO is reduced. Calculations with structures of Rhodobacter sphaeroides, Paracoccus denitrificans, and bovine CcO derived by crystallography and molecular dynamics show the PLS functions similarly in different CcO species. The PLS is a cluster rather than a single residue, as different structures show 1-4 residues load and release protons. However, the proton affinity of the heme a3 propionic acids primarily determines the number of protons loaded into the PLS; if their proton affinity is too low, less than one proton is loaded.
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.