Evidence map›Paper›PMID 35974100›Full record

ArticleNature communications2022

Hydrogen-bonded organic framework biomimetic entrapment allowing non-native biocatalytic activity in enzyme.

Guosheng Chen, Linjing Tong, Siming Huang, Shuyao Huang, Fang Zhu, Gangfeng Ouyang

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  8. Reticular Frameworks for Advanced Polymer Materials.Advanced materials (Deerfield Beach, Fla.) · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Design, Synthesis, and Application of Immobilized Enzymes on Artificial Porous Materials.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Electro-Driven Multi-Enzymatic Cascade Conversion of COAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  17. Article
  18. Review
  19. Review
  20. 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

6 authors.

Guosheng Chen *MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China. chengsh39@mail.sysu.edu.cn.ORCID http://orcid.org/0000-0002-6540-7675
Linjing Tong *MOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China.
Siming HuangGuangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences and the Fifth Affiliated Hospital, Guangzhou Medical University, Guangzhou, 511436, China.ORCID http://orcid.org/0000-0002-0912-1082
Shuyao HuangInstrumental Analysis and Research Center, Sun Yat-sen University, Guangzhou, 510275, China.
Fang ZhuMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China.
Gangfeng OuyangMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, 510275, China. cesoygf@mail.sysu.edu.cn.ORCID http://orcid.org/0000-0002-0797-6036

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nature programs the structural folding of an enzyme that allows its on-demand biofunctionality; however, it is still a long-standing challenge to manually modulate an enzyme's conformation. Here, we design an exogenous hydrogen-bonded organic framework to modulate the conformation of cytochrome c, and hence allow non-native bioactivity for the enzyme. The rigid hydrogen-bonded organic framework, with net-arranged carboxylate inner cage, is in situ installed onto the native cytochrome c. The resultant hydrogen-bonded nano-biointerface changes the conformation to a previously not achieved catalase-like species within the reported cytochrome c-porous organic framework systems. In addition, the preserved hydrogen-bonded organic framework can stabilize the encapsulated enzyme and its channel-like pores also guarantee the free entrance of catalytic substrates. This work describes a conceptual nanotechnology for manoeuvring the flexible conformations of an enzyme, and also highlights the advantages of artificial hydrogen-bonded scaffolds to modulate enzyme activity.

Indexed as

BiomimeticsHydrogenBiocatalysisCytochromes cHydrogen BondingCytochromes cHydrogen

Identifiers

PMID35974100
PMCPMC9381776

What OpenQuestion holds

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LicenceCC BY
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.