Evidence map›Paper›PMID 42446741›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2026

EPR characterization of a metal-binding site in RquA.

Rachelle K Stowell, Trilok Neupane, Kristian C Mankiller, Tanner L Manning, Lily N Boercker, Charlotte V DiGaetano, Lauren R Gotshall, Maegan N Burke, Andrew Ozarowski, Eric E Ross and 3 more

Abstract read
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Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Rachelle K StowellDepartment of Chemistry, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0001-7637-3442
Trilok NeupaneDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada.ORCID http://orcid.org/0000-0002-6524-9080
Kristian C MankillerDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Tanner L ManningDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Lily N BoerckerDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Charlotte V DiGaetanoDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Lauren R GotshallDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.
Maegan N BurkeDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada.ORCID http://orcid.org/0009-0001-7863-8229
Andrew OzarowskiNational High Magnetic Field Laboratory, Tallahassee, FL, USA.ORCID http://orcid.org/0000-0001-6225-9796
Eric E RossDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA.ORCID http://orcid.org/0000-0003-1820-5170
David N LangelaanDepartment of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, Canada. dlangela@dal.ca.ORCID http://orcid.org/0000-0001-9592-3075
Jennifer N ShepherdDepartment of Chemistry and Biochemistry, Gonzaga University, Spokane, WA, USA. shepherd@gonzaga.edu.ORCID http://orcid.org/0000-0002-6926-6777
Stefan StollDepartment of Chemistry, University of Washington, Seattle, WA, USA. stst@uw.edu.ORCID http://orcid.org/0000-0003-4255-9550

Funding

TRAINING IN MOLECULAR BIOPHYSICST32GM008268 · NIGMS · UNIVERSITY OF WASHINGTON · PI KOLLMAN, JUSTIN M, ZHENG, NING · 1988 to 2023
$8.6M
Canada Research Coordinating Committee NFRFE-2018-01643NIH HHS GM151956NIH HHS T32GM008268
6 · The paper itself

Abstract

Rhodoquinone (RQ) is a crucial electron carrier involved in anaerobic metabolism across select bacteria, protists, and animal species. Its biosynthesis is catalyzed by the rhodoquinone biosynthesis enzyme (RquA), a methyltransferase-like enzyme that uses S-adenosyl-L-methionine to transfer an amino group, converting ubiquinone (UQ) into RQ. The activity of RquA in vitro is enhanced by the presence of divalent metal cations. To probe the metal dependence of RquA, we characterized its interactions with Mn(II), Co(II), and Zn(II). We found that these metal cations bind to RquA with a 1:1 stoichiometry and that Mn(II) and Co(II) exhibited sub-micromolar binding affinities to RquA. Using Mn(II) as a spectroscopic probe, continuous‑wave electron paramagnetic resonance (EPR) revealed a single Mn(II) species with zero‑field splitting parameters |D| = 540(30) MHz and E/D = 0.30(3). Pulse EPR experiments on natural‑abundance and

Indexed as

CobaltManganeseMethyltransferasesBinding SitesElectron Spin Resonance SpectroscopyModels, MolecularZincCobaltManganeseMethyltransferasesZincEPRHYSCOREICP-MSITCmanganeseRquAS-adenosyl-L-methionine

Identifiers

PMID42446741

What OpenQuestion holds

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Registered trials

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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.