Evidence map›Paper›PMID 39409193›Full record

ArticleInternational journal of molecular sciences2024

Solid-State Nanopore-Based Nanosystem for Registration of Enzymatic Activity of a Single Molecule of Cytochrome P450 BM3.

Yuri D Ivanov, Angelina V Vinogradova, Ekaterina D Nevedrova, Alexander N Ableev, Andrey F Kozlov, Ivan D Shumov, Vadim S Ziborov, Oleg N Afonin, Nikita V Vaulin, Denis V Lebedev and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2024. 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

15 authors.

Yuri D IvanovInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.ORCID 0000-0001-5041-1914
Angelina V VinogradovaInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.ORCID 0009-0001-6044-3490
Ekaterina D NevedrovaInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.
Alexander N AbleevInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.
Andrey F KozlovInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.
Ivan D ShumovInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.ORCID 0000-0002-9795-7065
Vadim S ZiborovInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.
Oleg N AfoninInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.ORCID 0009-0008-7947-3674
Nikita V VaulinLaboratory of Renewable Energy Sources, St. Petersburg Academic University, 8/3, Khlopina St., 194021 St. Petersburg, Russia.ORCID 0000-0001-6080-0729
Denis V LebedevLaboratory of Renewable Energy Sources, St. Petersburg Academic University, 8/3, Khlopina St., 194021 St. Petersburg, Russia.ORCID 0000-0001-5389-2899
Anton S BukatinLaboratory of Renewable Energy Sources, St. Petersburg Academic University, 8/3, Khlopina St., 194021 St. Petersburg, Russia.ORCID 0000-0002-5459-1438
Polina K AfonichevaInstitute for Analytical Instrumentation RAS, 31-33 Lit. A, Ivana Chernykh St., 198095 St. Petersburg, Russia.
Ivan S MukhinLaboratory of Renewable Energy Sources, St. Petersburg Academic University, 8/3, Khlopina St., 194021 St. Petersburg, Russia.ORCID 0000-0001-9792-045X
Sergey A UsanovInstitute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 5/2, Kuprevich St., 220141 Minsk, Belarus.
Alexander I ArchakovInstitute of Biomedical Chemistry, 10, Pogodinskaya St., 119121 Moscow, Russia.

Funding

The Ministry of Science and Higher Education of the Russian Federation 075-15-2024-643
6 · The paper itself

Abstract

Experimental methods of single-molecule enzymology allow scientists to determine physicochemical properties of distinct single molecules of various enzymes and to perform direct monitoring of functioning of enzymes at different steps of their catalytic cycle. The approach based on the use of solid-state nanopores is a promising tool for studying the functioning of single-enzyme molecules. Herein, this approach is employed for monitoring the functioning of cytochrome P450 BM3, which represents a very convenient model of cytochrome P450-containing monooxygenase systems. A nanopore of ~5 nm in diameter has been formed in a 40 nm-thick silicon nitride chip by electron beam drilling (EBD), and a single molecule of the BM3 enzyme has been entrapped in the pore. The functioning of the enzyme molecule has been monitored by recording the time dependence of the ion current through the nanopore during the reaction of laurate hydroxylation. In our experiments, the enzyme molecule has been found to be active for 1500 s. The results of our research can be further used in the development of highly sensitive detectors for single-molecule studies in enzymology.

Indexed as

Cytochrome P-450 Enzyme SystemNanoporesBacterial ProteinsNADPH-Ferrihemoprotein ReductaseSingle Molecule ImagingBacterial ProteinsCytochrome P-450 Enzyme Systemflavocytochrome P450 BM3 monoxygenasesNADPH-Ferrihemoprotein Reductasecytochrome P450 BM3enzyme functioningnanopore detectorsolid-state nanopore

Identifiers

PMID39409193
PMCPMC11477413

What Socratic holds

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LicenceCC BY
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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 Socratic graph.