Evidence map›Paper›PMID 39810351›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2025

Electrochemical Small-Angle X-ray Scattering for Potential-Dependent Structural Analysis of Redox Enzymes.

Noya Loew, Chika Miura, Chiaki Sawahara, Saki Otobe, Taku Ogura, Yuichi Takasaki, Hikari Watanabe, Isao Shitanda, Masayuki Itagaki

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2025. 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

9 authors.

Noya LoewDepartment of Pure and Applied Chemistry, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
Chika MiuraDepartment of Pure and Applied Chemistry, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
Chiaki SawaharaDepartment of Pure and Applied Chemistry, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
Saki OtobeNikko Chemicals Co. Ltd., 3-24-3 Hasune, Itabashi-ku, Tokyo 174-0046, Japan.
Taku OguraNikko Chemicals Co. Ltd., 3-24-3 Hasune, Itabashi-ku, Tokyo 174-0046, Japan.ORCID 0000-0003-4205-2477
Yuichi TakasakiAnton Paar Japan K.K., Riverside Sumida 1F, 1-19-9, Tsutsumi-dori, Sumida-ku, Tokyo 131-0034, Japan.
Hikari WatanabeDepartment of Pure and Applied Chemistry, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.ORCID 0000-0002-1547-7042
Isao ShitandaDepartment of Pure and Applied Chemistry, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.ORCID 0000-0001-9751-016X
Masayuki ItagakiDepartment of Pure and Applied Chemistry, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Various methods exist for exploring different aspects of these mechanisms. However, techniques for investigating structural differences between the reduced and oxidized forms of an enzyme are limited. Here, we propose electrochemical small-angle X-ray scattering (EC-SAXS) as a novel method for potential-dependent structural analysis of redox enzymes and redox-active proteins. While similar approaches have been employed previously in battery and fuel cell research, biological samples have not yet been analyzed using this technique. Using EC-SAXS, we elucidated the structures of oxidized and reduced bilirubin oxidase (BOD). The oxidized BOD favors an open state, enhancing accessibility to the active center, whereas the reduced BOD prefers a closed state. EC-SAXS not only broadens our understanding of redox enzymes but also offers insights that could aid in developing customized enzyme immobilization strategies. These strategies could considerably improve the performance of biosensors, biofuel cells, and other bioelectronics.

Indexed as

Oxidoreductases Acting on CH-CH Group DonorsScattering, Small AngleX-Ray DiffractionElectrochemical TechniquesOxidation-Reductionbilirubin oxidaseOxidoreductases Acting on CH-CH Group Donors

Identifiers

PMID39810351
PMCPMC11736843

What Socratic holds

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LicenceCC BY
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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 Socratic graph.