Evidence map›Paper›PMID 30632592›Full record

ArticleDalton transactions (Cambridge, England : 2003)2019

Monitoring H-cluster assembly using a semi-synthetic HydF protein.

Brigitta Németh, Charlène Esmieu, Holly J Redman, Gustav Berggren

Open access · hybridAbstract read
In one paragraph

Article in Dalton transactions (Cambridge, England : 2003), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. In vitro maturation of fully active [FeFe]-hydrogenase in a defined system including the iron carrier NfuA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Article
  6. Organometallic FeJournal of the American Chemical Society · 2022
    Article
  7. HydG, the "dangler" iron, and catalytic production of free CO and CNDalton transactions (Cambridge, England : 2003) · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. [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
  12. H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019
    Article
  13. The final steps of [FeFe]-hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

4 authors at 1 institution in 1 country.

Brigitta NémethMolecular Biomimetics, Department of Chemistry -Ångström Laboratory, Uppsala University, 75120 Uppsala, Sweden. gustav.berggren@kemi.uu.se.
Charlène Esmieu
Holly J Redman
Gustav Berggren
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The [FeFe] hydrogenase enzyme interconverts protons and molecular hydrogen with remarkable efficiency. The reaction is catalysed by a unique metallo-cofactor denoted as the H-cluster containing an organometallic dinuclear Fe component, the [2Fe] subsite. The HydF protein delivers a precursor of the [2Fe] subsite to the apo-[FeFe] hydrogenase, thus completing the H-cluster and activating the enzyme. Herein we generate a semi-synthetic form of HydF by loading it with a synthetic low valent dinuclear Fe complex. We show that this semi-synthetic protein is practically indistinguishable from the native protein, and utilize this form of HydF to explore the mechanism of H-cluster assembly. More specifically, we show that transfer of the precatalyst from HydF to the hydrogenase enzyme results in the release of CO, underscoring that the pre-catalyst is a four CO species when bound to HydF. Moreover, we propose that an electron transfer reaction occurs during H-cluster assembly, resulting in an oxidation of the [2Fe] subsite with concomitant reduction of the [4Fe4S] cluster present on the HydF protein.

Indexed as

DimerizationProtonsCatalysisCatalytic DomainChlamydomonas reinhardtiiHemoglobinsHydrogenHydrogenaseOxidation-ReductionProtein ConformationHemoglobinsHydrogenHydrogenaseProtons

Identifiers

PMID30632592
PMCPMC6509880
OpenAlexW2908502653

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.