Evidence map›Paper›PMID 42443666›Full record

ArticleDoklady. Biochemistry and biophysics2026

The Kinetics of Intrinsic Luminescence of Bacterial Luciferase during Catalysis Indicates Flavin Binding and Enzyme Recovery.

A E Lisitsa, D V Gulnov, I V Shakhmatov, E A Kirichenko, L P Burakova, V A Kratasyuk, E V Nemtseva

Abstract read
PubMed Publisher
In one paragraph

Article in Doklady. Biochemistry and biophysics, 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

7 authors.

A E LisitsaSiberian Federal University, Krasnoyarsk, Russia. ALisitsa@sfu-kras.ru.
D V GulnovSiberian Federal University, Krasnoyarsk, Russia.
I V ShakhmatovSiberian Federal University, Krasnoyarsk, Russia.
E A KirichenkoSiberian Federal University, Krasnoyarsk, Russia.
L P BurakovaSiberian Federal University, Krasnoyarsk, Russia.
V A KratasyukSiberian Federal University, Krasnoyarsk, Russia.
E V NemtsevaSiberian Federal University, Krasnoyarsk, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study proposes an experimental approach to determining the rates of individual stages of a reaction catalyzed by bacterial luciferase, based on the tryptophan fluorescence of the protein and the stopped-flow technique. The relationship between the fluorescence intensity of tryptophan residues in luciferase and the presence of substrates and reaction products in the active site of the enzyme is substantiated. The non-steady-state kinetics of bioluminescence in the reaction of two bacterial luciferases with aliphatic aldehydes of different chain lengths, as well as the kinetics of enzyme fluorescence intensity during the reaction, were analyzed. The obtained results confirmed the relationship between the rate of the two kinetic stages of enzyme luminescence and the processes of flavin substrate binding and enzyme activity recovery after the catalytic act.

Indexed as

FlavinsLuciferases, BacterialCatalysisKineticsLuminescenceProtein BindingTryptophanFlavinsLuciferases, BacterialTryptophanbacterial luciferasebioluminescenceenzymatic catalysisprotein luminescencestopped-flow technique

Identifiers

PMID42443666

What OpenQuestion holds

Textmetadata
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.