Evidence map›Paper›PMID 33116131›Full record

ArticleNature communications2020

Reprogramming bacterial protein organelles as a nanoreactor for hydrogen production.

Tianpei Li, Qiuyao Jiang, Jiafeng Huang, Catherine M Aitchison, Fang Huang, Mengru Yang, Gregory F Dykes, Hai-Lun He, Qiang Wang, Reiner Sebastian Sprick and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
7.3field-weighted citation impact, top 2% of its field
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

72 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. A Generative Neuro-Symbolic AI for Protein Sequence Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Review
  5. Review
  6. Review
  7. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
    Review
  8. Review
  9. Chemical reviews · 2026
    Review
  10. Architectural and biochemical advances in understanding microbial COThe Plant journal : for cell and molecular biology · 2026
    Review
  11. Article
  12. Article
  13. Control of encounter kinetics by chemically active droplets.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Review
  15. Structure and encapsulation of carbonic anhydrase within the α-carboxysome.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Engineering COInternational journal of molecular sciences · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

12 more citing papers are in PubMed but not listed here.

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

12 authors at 3 institutions in 2 countries.

Tianpei LiInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Qiuyao JiangInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Jiafeng HuangInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Catherine M AitchisonMaterials Innovation Factory and Department of Chemistry, University of Liverpool, Liverpool, L7 3NY, UK.
Fang HuangInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Mengru YangInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Gregory F DykesInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.ORCID 0000-0002-0626-9487
Hai-Lun HeSchool of Life Sciences, Central South University, Changsha, China.
Qiang WangState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan University, 475004, Kaifeng, China. wangqiang@henu.edu.cn.
Reiner Sebastian SprickMaterials Innovation Factory and Department of Chemistry, University of Liverpool, Liverpool, L7 3NY, UK.
Andrew I CooperMaterials Innovation Factory and Department of Chemistry, University of Liverpool, Liverpool, L7 3NY, UK.ORCID 0000-0003-0201-1021
Lu-Ning LiuInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK. luning.liu@liverpool.ac.uk.ORCID 0000-0002-8884-4819
University of Liverpool · GBCentral South University · CNHenan University · CN

Funding

Biotechnology and Biological Sciences Research Council BB/M024202/1Biotechnology and Biological Sciences Research Council BB/R003890/1
6 · The paper itself

Abstract

Compartmentalization is a ubiquitous building principle in cells, which permits segregation of biological elements and reactions. The carboxysome is a specialized bacterial organelle that encapsulates enzymes into a virus-like protein shell and plays essential roles in photosynthetic carbon fixation. The naturally designed architecture, semi-permeability, and catalytic improvement of carboxysomes have inspired rational design and engineering of new nanomaterials to incorporate desired enzymes into the protein shell for enhanced catalytic performance. Here, we build large, intact carboxysome shells (over 90 nm in diameter) in the industrial microorganism Escherichia coli by expressing a set of carboxysome protein-encoding genes. We develop strategies for enzyme activation, shell self-assembly, and cargo encapsulation to construct a robust nanoreactor that incorporates catalytically active [FeFe]-hydrogenases and functional partners within the empty shell for the production of hydrogen. We show that shell encapsulation and the internal microenvironment of the new catalyst facilitate hydrogen production of the encapsulated oxygen-sensitive hydrogenases. The study provides insights into the assembly and formation of carboxysomes and paves the way for engineering carboxysome shell-based nanoreactors to recruit specific enzymes for diverse catalytic reactions.

Indexed as

BioreactorsBacterial ProteinsBiocatalysisBioengineeringEscherichia coliGenes, BacterialHalothiobacillusHydrogenHydrogenaseIron-Sulfur ProteinsNanocapsulesOrganellesPhotosynthesisRibulose-Bisphosphate CarboxylaseBacterial ProteinsHydrogenHydrogenaseiron hydrogenaseIron-Sulfur ProteinsNanocapsulesRibulose-Bisphosphate Carboxylase

Identifiers

PMID33116131
PMCPMC7595155
OpenAlexW3096668248

What OpenQuestion holds

Textmetadata
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.