Evidence map›Paper›PMID 39888997›Full record

ArticleScience advances2025

Single molecule-driven nanomotors reveal the dynamic-disordered chemomechanical transduction of active enzymes.

Zhuodong Tang, Jingyu Wu, Shaojun Wu, Wenjing Tang, Jian-Rong Zhang, Wenlei Zhu, Jun-Jie Zhu, Zixuan Chen

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

8 authors.

Zhuodong TangState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.ORCID 0009-0006-2761-5031
Jingyu WuState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.
Shaojun WuState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.
Wenjing TangState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.ORCID 0009-0000-5352-6530
Jian-Rong ZhangState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.
Wenlei ZhuState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.ORCID 0000-0001-6110-993X
Jun-Jie ZhuState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.ORCID 0000-0002-8201-1285
Zixuan ChenState Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, State Key Laboratory of Pollution Control and Resource Reuse, School of Environment, Nanjing University, 163 Xianlin Ave., Nanjing 210023, China.ORCID 0000-0002-3017-1121

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes facilitate the conversion of chemical energy into mechanical work during biochemical reactions, thereby regulating the dynamic metabolic activity of living systems. However, directly observing the energy release facilitated by fluctuating individual enzymes remains a challenge, leading to a contentious debate regarding the underlying reasons for this phenomenon. Here, we aim to overcome this challenge by developing an oscillating nanomotor powered by a single-molecule enzyme, which allows real-time tracking of energy transduction in enzymatic reactions. Through analysis of the shifts in free energy profiles within the nanomotors, our results unveil not only the heterogeneous energy release patterns of individual enzyme molecules but also the dynamic disorder of a particular enzyme in energy release over extended monitoring periods. By exploring six distinct types of single-molecule enzymatic reactions, we provide the direct evidence supporting the argument that the reaction enthalpy governs the enzymatic energy release. This approach has implications for understanding the mechanism of enzymatic catalysis and developing highly efficient nanomotors.

Indexed as

EnzymesNanostructuresBiocatalysisNanotechnologyThermodynamicsEnzymes

Identifiers

PMID39888997
PMCPMC11784849

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.