Evidence map›Paper›PMID 31733183›Full record

ArticleBiochimica et biophysica acta. Bioenergetics2020

Structural changes at the surface of cytochrome c oxidase alter the proton-pumping stoichiometry.

Johan Berg, Jian Liu, Emelie Svahn, Shelagh Ferguson-Miller, Peter Brzezinski

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Bioenergetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
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

5 authors at 2 institutions in 2 countries.

Johan BergDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-106 91 Stockholm, Sweden.
Jian LiuDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, United States.
Emelie SvahnDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-106 91 Stockholm, Sweden.
Shelagh Ferguson-MillerDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, United States. Electronic address: fergus20@msu.edu.
Peter BrzezinskiDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-106 91 Stockholm, Sweden. Electronic address: peterb@dbb.su.se.
Stockholm University · SEMichigan State University · US

Funding

ORGANIZATION AND CONTROL OF ELECTRON TRANSFER CHAINSR01GM026916 · NIGMS · MICHIGAN STATE UNIVERSITY · PI FERGUSON-MILLER, SHELAGH M · 1985 to 2014
$1.6M
NIGMS NIH HHS R01 GM026916
6 · The paper itself

Abstract

Data from earlier studies showed that minor structural changes at the surface of cytochrome c oxidase, in one of the proton-input pathways (the D pathway), result in dramatically decreased activity and a lower proton-pumping stoichiometry. To further investigate how changes around the D pathway orifice influence functionality of the enzyme, here we modified the nearby C-terminal loop of subunit I of the Rhodobacter sphaeroides cytochrome c oxidase. Removal of 16 residues from this flexible surface loop resulted in a decrease in the proton-pumping stoichiometry to <50% of that of the wild-type enzyme. Replacement of the protonatable residue Glu552, part of the same loop, by an Ala, resulted in a similar decrease in the proton-pumping stoichiometry without loss of the O

Indexed as

Bacterial ProteinsElectron Transport Complex IVProtein Structure, SecondaryRhodobacter sphaeroidesBacterial ProteinsElectron Transport Complex IVActinobacteriaElectron transferMitochondriaMycobacterium smegmatisProton pumpingRespiratory chain

Identifiers

PMID31733183
PMCPMC6943178
OpenAlexW2984916540

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.