ArticleProceedings of the National Academy of Sciences of the United States of America2003
Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 91 citations in OpenAlex.
- Proton-Coupled Electron Transfer in Cytochrome c Oxidase: Heme a Controls the Protonation Dynamics of E286.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Electric fields control water-gated proton transfer in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy.Frontiers in molecular biosciences · 2022Article
- Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies.Molecules (Basel, Switzerland) · 2021Review
- Quantification of Local Electric Field Changes at the Active Site of CytochromeFrontiers in chemistry · 2021Article
- How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.Journal of the American Chemical Society · 2019Article
- 2Chemical science · 2015Article
- Microscopic basis for kinetic gating in Cytochrome c oxidase: insights from QM/MM analysis.Chemical science · 2015Article
- Proton translocation in cytochrome c oxidase: insights from proton exchange kinetics and vibrational spectroscopy.Biochimica et biophysica acta · 2015Review
- Proton transfer and protein conformation dynamics in photosensitive proteins by time-resolved step-scan Fourier-transform infrared spectroscopy.Journal of visualized experiments : JoVE · 2014Article
- Phase-sensitive detection in modulation excitation spectroscopy applied to potential induced electron transfer in cytochrome c oxidase.Applied spectroscopy · 2014Article
- Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.Biophysical journal · 2013Article
- Design of photoactive ruthenium complexes to study electron transfer and proton pumping in cytochrome oxidase.Biochimica et biophysica acta · 2012Review
- 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer.Metallomics : integrated biometal science · 2011Article
- Synthesis of a cyclic pentapeptide mimic of the active site His-Tyr cofactor of cytochrome c oxidase.The Journal of organic chemistry · 2009Article
- A spectroscopic investigation of a tridentate Cu-complex mimicking the tyrosine-histidine cross-link of cytochrome C oxidase.The journal of physical chemistry. B · 2009Article
- Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba3 of Thermus thermophilus.Journal of the American Chemical Society · 2008Article
- A chemically explicit model for the mechanism of proton pumping in heme-copper oxidases.Journal of bioenergetics and biomembranes · 2008Article
- Glutamic acid 242 is a valve in the proton pump of cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Redox-coupled proton pumping in cytochrome c oxidase: further insights from computer simulation.Biochimica et biophysica acta · 2008Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cytochrome c oxidase, the terminal protein in the respiratory chain, converts oxygen into water and helps generate the electrochemical gradient used in the synthesis of ATP. The catalytic action of cytochrome c oxidase involves electron transfer, proton transfer, and O2 reduction. These events trigger specific molecular changes at the active site, which, in turn, influence changes throughout the protein, including alterations of amino acid side chain orientations, hydrogen bond patterns, and protonation states. We have used IR difference spectroscopy to investigate such modulations for the functional intermediate states E, R2,Pm, and F. These spectra reveal deprotonation of its key glutamic acid E286 in the E and in the Pm states. The consecutive deprotonation and reprotonation of E286 twice within one catalytic turnover illustrates the role of this residue as a proton shuttle. In addition, the spectra point toward deprotonation of a redox-active tyrosine, plausibly Y288, in the F intermediate. Structural insights into the molecular mechanism of catalysis based on the subtle molecular changes observed with IR difference spectroscopy are discussed.
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.