Evidence map›Paper›PMID 35072518›Full record

ArticleJournal of bacteriology2022

Dissection and Reconstitution Provide Insights into Electron Transport in the Membrane-Bound Aldehyde Dehydrogenase Complex of Gluconacetobacter diazotrophicus.

Roni Miah, Shun Nina, Takeru Murate, Naoya Kataoka, Minenosuke Matsutani, Yoshitaka Ano, Kazunobu Matsushita, Toshiharu Yakushi

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 50% 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

4 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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

8 authors at 3 institutions in 1 country.

Roni MiahDivision of Life Science, Graduate School of Sciences and Technology for Innovation, Yamaguchi Universitygrid.268397.1, Yamaguchi, Japan.
Shun NinaDepartment of Biological Chemistry, Faculty of Agriculture, Yamaguchi Universitygrid.268397.1, Yamaguchi, Japan.
Takeru MurateDivision of Life Science, Graduate School of Sciences and Technology for Innovation, Yamaguchi Universitygrid.268397.1, Yamaguchi, Japan.
Naoya KataokaDivision of Life Science, Graduate School of Sciences and Technology for Innovation, Yamaguchi Universitygrid.268397.1, Yamaguchi, Japan.
Minenosuke MatsutaniNODAI Genome Research Center, Tokyo University of Agriculture, Tokyo, Japan.ORCID 0000-0002-6262-3188
Yoshitaka AnoDepartment of Bioscience, Graduate School of Agriculture, Ehime Universitygrid.255464.4, Matsuyama, Japan.
Kazunobu MatsushitaDivision of Life Science, Graduate School of Sciences and Technology for Innovation, Yamaguchi Universitygrid.268397.1, Yamaguchi, Japan.
Toshiharu YakushiDivision of Life Science, Graduate School of Sciences and Technology for Innovation, Yamaguchi Universitygrid.268397.1, Yamaguchi, Japan.ORCID 0000-0003-2279-8968
Yamaguchi University · JPEhime University · JPTokyo University of Agriculture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetic acid bacteria catalyze the two-step oxidation of ethanol to acetic acid using the membrane-bound enzymes pyrroloquinoline quinone-dependent alcohol dehydrogenase and molybdopterin-dependent aldehyde dehydrogenase (ALDH). Although the reducing equivalents from the substrate are transferred to ubiquinone in the membrane, intramolecular electron transport in ALDH is not understood. Here, we purified the AldFGH complex, the membrane-bound ALDH that is physiologically relevant to acetic acid fermentation in Gluconacetobacter diazotrophicus strain PAL5. The purified AldFGH complex showed acetaldehyde:ubiquinone (Q

Indexed as

Alcohol DehydrogenaseAldehyde DehydrogenaseAcetaldehydeAcetic AcidAldehydesCytochromesElectron TransportGluconacetobacterPQQ CofactorUbiquinoneAcetaldehydeAcetic AcidAlcohol DehydrogenaseAldehyde DehydrogenaseAldehydesCytochromesPQQ CofactorUbiquinoneacetic acid fermentationcytochrome c[Fe-S] clusterGluconacetobacter diazotrophicusmembrane-bound aldehyde dehydrogenase

Identifiers

PMID35072518
PMCPMC8923213
OpenAlexW4207019399

What OpenQuestion holds

Textmetadata
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.