Evidence map›Paper›PMID 39300852›Full record

ArticleSmall methods2025

Electrochemically Induced Nanoscale Stirring Boosts Functional Immobilization of Flavocytochrome P450 BM3 on Nanoporous Gold Electrodes.

Elisabeth Hengge, Eva-Maria Steyskal, Alexander Dennig, Manfred Nachtnebel, Harald Fitzek, Roland Würschum, Bernd Nidetzky

Abstract read
In one paragraph

Article in Small methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
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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

7 authors.

Elisabeth HenggeInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, Graz, 8010, Austria.
Eva-Maria SteyskalInstitute of Materials Physics, Graz University of Technology, Petergasse 16, Graz, 8010, Austria.
Alexander DennigInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, Graz, 8010, Austria.
Manfred NachtnebelGraz Centre for Electron Microscopy (ZFE), Steyrergasse 17, Graz, 8010, Austria.
Harald FitzekGraz Centre for Electron Microscopy (ZFE), Steyrergasse 17, Graz, 8010, Austria.
Roland WürschumInstitute of Materials Physics, Graz University of Technology, Petergasse 16, Graz, 8010, Austria.
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, Graz, 8010, Austria.ORCID 0000-0002-5030-2643

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme-modified electrodes are core components of electrochemical biosensors for diagnostic and environmental analytics and have promising applications in bioelectrocatalysis. Despite huge research efforts spanning decades, design of enzyme electrodes for superior performance remains challenging. Nanoporous gold (npAu) represents advanced electrode material due to high surface-to-volume ratio, tunable porosity, and intrinsic redox activity, yet its coupling with enzyme catalysis is complex. Here, the study reports a flexible-modular approach to modify npAu with functional enzymes by combined material and protein engineering and use a tailored assortment of surface and in-solution methodologies for characterization. Self-assembled monolayer (SAM) of mercaptoethanesulfonic acid primes the npAu surface for electrostatic adsorption of the target enzyme (flavocytochrome P450 BM3; CYT102A1) that is specially equipped with a cationic protein module for directed binding to anionic surfaces. Modulation of the SAM surface charge is achieved by electrochemistry. The electrode-adsorbed enzyme retains well the activity (33%) and selectivity (complete) from in-solution. Electrochemically triggered nanoscale stirring in the internal porous network of npAu-SAM enhances speed (2.5-fold) and yield (3.0-fold) of the enzyme immobilization. Biocatalytic reaction is fueled from the electrode via regeneration of its reduced coenzyme (NADPH). Collectively, the study presents a modular design of npAu-based enzyme electrode that can support flexible bioelectrochemistry applications.

Indexed as

Bacterial ProteinsCytochrome P-450 Enzyme SystemElectrochemical TechniquesEnzymes, ImmobilizedGoldNADPH-Ferrihemoprotein ReductaseNanoporesBiosensing TechniquesElectrodesPorosityBacterial ProteinsCytochrome P-450 Enzyme SystemEnzymes, Immobilizedflavocytochrome P450 BM3 monoxygenasesGoldNADPH-Ferrihemoprotein Reductasebioelectrochemistry and biosensingbiointerface engineeringcharge‐directed functional immobilizationenzyme electrodeflavocytochrome P450nanoporous goldself‐assembled monolayer

Identifiers

PMID39300852
PMCPMC11926518

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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.