Evidence map›Paper›PMID 20356731›Full record

ArticleCurrent opinion in biotechnology2010

Artificial hydrogenases.

Bryan E Barton, Matthew T Olsen, Thomas B Rauchfuss

Abstract read
In one paragraph

Article in Current opinion in biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.Journal of the American Chemical Society · 2019
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. 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

3 authors.

Bryan E BartonSchool of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States.
Matthew T Olsen
Thomas B Rauchfuss

Funding

FE-S ENSEMBLES RELATED TO HYDROGENASE ACTIVITYR01GM061153 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RAUCHFUSS, THOMAS · 2000 to 2025
$6.7M
NIGMS NIH HHS R01 GM061153
6 · The paper itself

Abstract

Decades of biophysical study on the hydrogenase (H(2)ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H(2)ases, [NiFe]-H(2)ases, and [Fe]-H(2)ases, all of which feature iron centers bound to both CO and thiolate. Artificial H(2)ases affect the oxidation of H(2) and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H(2) toward biomimetic H(2)ases.

Indexed as

BiomimeticsHydrogenHydrogenaseIronIron-Sulfur ProteinsHydrogenHydrogenaseIronIron-Sulfur Proteins

Identifiers

PMID20356731
PMCPMC2903054

What OpenQuestion holds

Textmetadata
LicenceTDM
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.