Evidence map›Paper›PMID 23507617›Full record

ReviewBiochimica et biophysica acta

Molecular mechanisms for generating transmembrane proton gradients.

M R Gunner, Muhamed Amin, Xuyu Zhu, Jianxun Lu

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 54 citations in OpenAlex.

  1. Redox-Activated Proton Transfer through a Redundant Network in the QJournal of chemical information and modeling · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. O to bR transition in bacteriorhodopsin occurs through a proton hole mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Review
  9. Cavity hydration dynamics in cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Review
  11. Article
  12. Article
  13. Halorhodopsin pumps Cl- and bacteriorhodopsin pumps protons by a common mechanism that uses conserved electrostatic interactions.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Characterizing the proton loading site in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Changing hydration level in an internal cavity modulates the proton affinity of a key glutamate in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

M R GunnerDepartment of Physics, City College of New York, New York, NY 10031, USA. gunner@sci.ccny.cuny.edu
Muhamed Amin
Xuyu Zhu
Jianxun Lu
City College of New York · US

Funding

TNC FUNCTION IN APOPTOTIC ANTIGEN DRIVEN AUTOIMMUNITYG12RR003060 · NCRR · CITY COLLEGE OF NEW YORK · PI WALLMAN, JOSHUA · 1985 to 2011
$26.1M
Cellular/Molecular Basis of Development: Research CenterG12MD007603 · NIMHD · CITY COLLEGE OF NEW YORK · PI PEZZANO, MARK · 2012 to 2017
$11.5M
NCRR NIH HHS G12 RR003060NCRR NIH HHS G12RR03060NIMHD NIH HHS G12 MD007603NIMHD NIH HHS G12MD007603
6 · The paper itself

Abstract

Membrane proteins use the energy of light or high energy substrates to build a transmembrane proton gradient through a series of reactions leading to proton release into the lower pH compartment (P-side) and proton uptake from the higher pH compartment (N-side). This review considers how the proton affinity of the substrates, cofactors and amino acids are modified in four proteins to drive proton transfers. Bacterial reaction centers (RCs) and photosystem II (PSII) carry out redox chemistry with the species to be oxidized on the P-side while reduction occurs on the N-side of the membrane. Terminal redox cofactors are used which have pKas that are strongly dependent on their redox state, so that protons are lost on oxidation and gained on reduction. Bacteriorhodopsin is a true proton pump. Light activation triggers trans to cis isomerization of a bound retinal. Strong electrostatic interactions within clusters of amino acids are modified by the conformational changes initiated by retinal motion leading to changes in proton affinity, driving transmembrane proton transfer. Cytochrome c oxidase (CcO) catalyzes the reduction of O2 to water. The protons needed for chemistry are bound from the N-side. The reduction chemistry also drives proton pumping from N- to P-side. Overall, in CcO the uptake of 4 electrons to reduce O2 transports 8 charges across the membrane, with each reduction fully coupled to removal of two protons from the N-side, the delivery of one for chemistry and transport of the other to the P-side.

Indexed as

BacteriorhodopsinsCatalysisElectron Transport Complex IVHydrogen-Ion ConcentrationMembrane ProteinsModels, MolecularOxidation-ReductionPhotosystem II Protein ComplexProtonsStatic ElectricityBacteriorhodopsinsElectron Transport Complex IVMembrane ProteinsPhotosystem II Protein ComplexProtonsBacterial reaction centersBacteriorhodopsinCytochrome c oxidaseMn clustersPhotosystem II

Identifiers

PMID23507617
PMCPMC3714358
OpenAlexW2077981096

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.