Evidence map›Paper›PMID 26862221›Full record

ReviewBiochemical Society transactions2016

Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases.

Lindsey A Flanagan, Alison Parkin

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2016. 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
2.6field-weighted citation impact, top 10% 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, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Spectroscopic elucidation of energy transfer in hybrid inorganic-biological organisms for solar-to-chemical production.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Biosynthesis of Salmonella enterica [NiFe]-hydrogenase-5: probing the roles of system-specific accessory proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  14. 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

2 authors at 1 institution in 1 country.

Lindsey A FlanaganDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K.
Alison ParkinDepartment of Chemistry, University of York, Heslington, York YO10 5DD, U.K. 2013 Early Career Research Award, Theme Panel III Energy and Metabolism alison.parkin@york.ac.uk.
University of York · GB

Funding

Wellcome Trust WT095024MA
6 · The paper itself

Abstract

Hydrogenases are enzymes of great biotechnological relevance because they catalyse the interconversion of H2, water (protons) and electricity using non-precious metal catalytic active sites. Electrochemical studies into the reactivity of NiFe membrane-bound hydrogenases (MBH) have provided a particularly detailed insight into the reactivity and mechanism of this group of enzymes. Significantly, the control centre for enabling O2 tolerance has been revealed as the electron-transfer relay of FeS clusters, rather than the NiFe bimetallic active site. The present review paper will discuss how electrochemistry results have complemented those obtained from structural and spectroscopic studies, to present a complete picture of our current understanding of NiFe MBH.

Indexed as

ElectrochemistryAmino Acid SequenceCatalytic DomainCell MembraneElectron TransportHydrogenaseModels, BiologicalMolecular Sequence DataHydrogenasenickel-iron hydrogenaseiron–sulfur cluster relaymembrane-bound hydrogenaseNiFe hydrogenaseoxygen toleranceprotein film electrochemistry

Identifiers

PMID26862221
PMCPMC4747160
OpenAlexW2252720155

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.