Evidence map›Paper›PMID 36697674›Full record

ArticleCommunications chemistry2022

Microbial rhodoquinone biosynthesis proceeds via an atypical RquA-catalyzed amino transfer from S-adenosyl-L-methionine to ubiquinone.

Trilok Neupane, Lydia R Chambers, Alexander J Godfrey, Melina M Monlux, Evan J Jacobs, Sophia Whitworth, Jamie E Spawn, Seo Hee K Clingman, Kathleen L Vergunst, Fair M Niven and 7 more

Open access · goldAbstract read
In one paragraph

Article in Communications chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 56% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. EPR characterization of a metal-binding site in RquA.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Natural product reports · 2023
    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

17 authors at 2 institutions in 2 countries.

Trilok NeupaneDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, Canada.ORCID http://orcid.org/0000-0002-6524-9080
Lydia R ChambersDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Alexander J GodfreyDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Melina M MonluxDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Evan J JacobsDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Sophia WhitworthDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Jamie E SpawnDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Seo Hee K ClingmanDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Kathleen L VergunstDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, Canada.
Fair M NivenDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
James J TownleyDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Iris W OrionDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Carly R GoodspeedDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Kathryn A CooperDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Jeff D CronkDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Jennifer N ShepherdDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA. shepherd@gonzaga.edu.ORCID http://orcid.org/0000-0002-6926-6777
David N LangelaanDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS, Canada. david.langelaan@dal.ca.ORCID http://orcid.org/0000-0001-9592-3075
Gonzaga University · USDalhousie University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rhodoquinone (RQ) is a close analogue of ubiquinone (UQ) that confers diverse bacterial and eukaryotic taxa the ability to utilize fumarate as an electron acceptor in hypoxic conditions. The RquA protein, identified in a Rhodospirillum rubrum RQ-deficient mutant, has been shown to be required for RQ biosynthesis in bacteria. In this report, we demonstrate that RquA, homologous to SAM-dependent methyltransferases, is necessary and sufficient to catalyze RQ biosynthesis from UQ in vitro. Remarkably, we show that RquA uses SAM as the amino group donor in a substitution reaction that converts UQ to RQ. In contrast to known aminotransferases, RquA does not use pyridoxal 5'-phosphate (PLP) as a coenzyme, but requires the presence of Mn

Identifiers

PMID36697674
PMCPMC9814641
OpenAlexW4289340044

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.