Evidence map›Paper›PMID 34123117›Full record

ArticleChemical science2020

Metal-ligand cooperativity in the soluble hydrogenase-1 from

Gregory E Vansuch, Chang-Hao Wu, Dominik K Haja, Soshawn A Blair, Bryant Chica, Michael K Johnson, Michael W W Adams, R Brian Dyer

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

8 authors at 3 institutions in 2 countries.

Gregory E VansuchDepartment of Chemistry, Emory University Atlanta Georgia 30222 USA briandyer@emory.edu.
Chang-Hao WuDepartment of Biochemistry & Molecular Biology, University of Georgia Athens Georgia 30602 USA.
Dominik K HajaDepartment of Biochemistry & Molecular Biology, University of Georgia Athens Georgia 30602 USA.
Soshawn A BlairDepartment of Chemistry, University of Georgia Athens Georgia 30602 USA.
Bryant ChicaDepartment of Chemistry, Emory University Atlanta Georgia 30222 USA briandyer@emory.edu.
Michael K JohnsonDepartment of Chemistry, University of Georgia Athens Georgia 30602 USA.
Michael W W AdamsDepartment of Biochemistry & Molecular Biology, University of Georgia Athens Georgia 30602 USA.
R Brian DyerDepartment of Chemistry, Emory University Atlanta Georgia 30222 USA briandyer@emory.edu.ORCID https://orcid.org/0000-0002-0090-7580
University of Georgia · USEmory University · USNational Laboratory of the Rockies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metal-ligand cooperativity is an essential feature of bioinorganic catalysis. The design principles of such cooperativity in metalloenzymes are underexplored, but are critical to understand for developing efficient catalysts designed with earth abundant metals for small molecule activation. The simple substrate requirements of reversible proton reduction by the [NiFe]-hydrogenases make them a model bioinorganic system. A highly conserved arginine residue (R355) directly above the exogenous ligand binding position of the [NiFe]-catalytic core is known to be essential for optimal function because mutation to a lysine results in lower catalytic rates. To expand on our studies of soluble hydrogenase-1 from

Identifiers

PMID34123117
PMCPMC8163435
OpenAlexW3046650494

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.