Evidence map›Paper›PMID 29334424›Full record

ArticleAngewandte Chemie (International ed. in English)2018

In Vivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases.

Lívia S Mészáros, Brigitta Németh, Charlène Esmieu, Pierre Ceccaldi, Gustav Berggren

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Light-Driven [FeFe] Hydrogenase Based HACS sustainable chemistry & engineering · 2022
    Article
  4. Article
  5. Article
  6. Stability of the H-cluster under whole-cell conditions-formation of an HJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Article
  7. Article
  8. [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  9. Article
  10. Article
  11. Monitoring H-cluster assembly using a semi-synthetic HydF protein.Dalton transactions (Cambridge, England : 2003) · 2019
    Article
  12. Article
  13. Review
  14. In Vivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases.Angewandte Chemie (International ed. in English) · 2018
    Article
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

5 authors at 1 institution in 1 country.

Lívia S MészárosDepartment of Chemistry-, Uppsala University, Lägerhyddsvägen 1, 75120, Uppsala, Sweden.ORCID 0000-0002-6681-4440
Brigitta NémethDepartment of Chemistry-, Uppsala University, Lägerhyddsvägen 1, 75120, Uppsala, Sweden.
Charlène EsmieuDepartment of Chemistry-, Uppsala University, Lägerhyddsvägen 1, 75120, Uppsala, Sweden.
Pierre CeccaldiDepartment of Chemistry-, Uppsala University, Lägerhyddsvägen 1, 75120, Uppsala, Sweden.
Gustav BerggrenDepartment of Chemistry-, Uppsala University, Lägerhyddsvägen 1, 75120, Uppsala, Sweden.ORCID 0000-0002-6717-6612
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EPR spectroscopy reveals the formation of two different semi-synthetic hydrogenases in vivo. [FeFe] hydrogenases are metalloenzymes that catalyze the interconversion of molecular hydrogen and protons. The reaction is catalyzed by the H-cluster, consisting of a canonical iron-sulfur cluster and an organometallic [2Fe] subsite. It was recently shown that the enzyme can be reconstituted with synthetic cofactors mimicking the composition of the [2Fe] subsite, resulting in semi-synthetic hydrogenases. Herein, we employ EPR spectroscopy to monitor the formation of two such semi-synthetic enzymes in whole cells. The study provides the first spectroscopic characterization of semi-synthetic hydrogenases in vivo, and the observation of two different oxidized states of the H-cluster under intracellular conditions. Moreover, these findings underscore how synthetic chemistry can be a powerful tool for manipulation and examination of the hydrogenase enzyme under in vivo conditions.

Indexed as

Chlamydomonas reinhardtiiElectron Spin Resonance SpectroscopyEscherichia coliHydrogenaseIron-Sulfur ProteinsModels, MolecularHydrogenaseiron hydrogenaseIron-Sulfur Proteinsartificial enzymesEPR spectroscopy[FeFe] hydrogenasemetalloenzymes

Identifiers

PMID29334424
PMCPMC6282530
OpenAlexW2783411755

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.