Evidence map›Paper›PMID 37239950›Full record

ReviewInternational journal of molecular sciences2023

Enzymatic and Bioinspired Systems for Hydrogen Production.

Linda Leone, Gianmattia Sgueglia, Salvatore La Gatta, Marco Chino, Flavia Nastri, Angela Lombardi

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Review
  3. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  4. Review
  5. Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Engineering bionanoreactor in bacteria for efficient hydrogen production.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. 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.

Linda LeoneDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0001-7293-1814
Gianmattia SguegliaDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.
Salvatore La GattaDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0003-0005-5557
Marco ChinoDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0002-0436-3293
Flavia NastriDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0002-3390-9822
Angela LombardiDepartment of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy.ORCID 0000-0002-2013-3009

Funding

European Union - NextGenerationEU; National Recovery and Resilience Plan (NRRP), Mission 4 Component 2 Investment 1.3 Project code PE0000021, Concession Decree No. 1561 of 11.10.2022 adopted by Ministero dell'Università e della Ricerca (MUR), CUP - E63C22002160007
6 · The paper itself

Abstract

The extraordinary potential of hydrogen as a clean and sustainable fuel has sparked the interest of the scientific community to find environmentally friendly methods for its production. Biological catalysts are the most attractive solution, as they usually operate under mild conditions and do not produce carbon-containing byproducts. Hydrogenases promote reversible proton reduction to hydrogen in a variety of anoxic bacteria and algae, displaying unparallel catalytic performances. Attempts to use these sophisticated enzymes in scalable hydrogen production have been hampered by limitations associated with their production and stability. Inspired by nature, significant efforts have been made in the development of artificial systems able to promote the hydrogen evolution reaction, via either electrochemical or light-driven catalysis. Starting from small-molecule coordination compounds, peptide- and protein-based architectures have been constructed around the catalytic center with the aim of reproducing hydrogenase function into robust, efficient, and cost-effective catalysts. In this review, we first provide an overview of the structural and functional properties of hydrogenases, along with their integration in devices for hydrogen and energy production. Then, we describe the most recent advances in the development of homogeneous hydrogen evolution catalysts envisioned to mimic hydrogenases.

Indexed as

HydrogenaseProtonsCatalysisHydrogenOxidation-ReductionPhotosynthesisHydrogenHydrogenaseProtonsartificial enzymesbiofuel cellsbioinspired catalysishydrogenhydrogenaseshydrogen-evolving catalystsphotocatalytic hydrogensmall-molecule complexessustainable energy production

Identifiers

PMID37239950
PMCPMC10218252

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.