Evidence map›Paper›PMID 27406946›Full record

ArticleChemical communications (Cambridge, England)2016

An internal electron reservoir enhances catalytic CO2 reduction by a semisynthetic enzyme.

Camille R Schneider, Hannah S Shafaat

Open access · greenAbstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

7 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Light-Driven COFrontiers in molecular biosciences · 2021
    Article
  4. Review
  5. The good, the neutral, and the positive: buffer identity impacts CODalton transactions (Cambridge, England : 2003) · 2019
    Article
  6. A photoactive semisynthetic metalloenzyme exhibits complete selectivity for COChemical communications (Cambridge, England) · 2018
    Article
  7. 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

2 authors at 1 institution in 1 country.

Camille R SchneiderDepartment of Chemistry and Biochemistry and Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. Shafaat.1@osu.edu.
Hannah S ShafaatDepartment of Chemistry and Biochemistry and Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. Shafaat.1@osu.edu.
The Ohio State University · US

Funding

CHEMISTRY/BIOLOGY TRAINING GRANTT32GM008512 · NIGMS · OHIO STATE UNIVERSITY · PI PEI, DEHUA · 1996 to 2016
$3.9M
NIGMS NIH HHS T32 GM008512
6 · The paper itself

Abstract

The development of an artificial metalloenzyme for CO2 reduction is described. The small-molecule catalyst [Ni(II)(cyclam)](2+) has been incorporated within azurin. Selectivity for CO generation over H(+) reduction is enhanced within the protein environment, while the azurin active site metal impacts the electrochemical overpotential and photocatalytic activity. The enhanced catalysis observed for copper azurin suggests an important role for intramolecular electron transfer, analogous to native CO2 reducing enzymes.

Indexed as

ElectronsAzurinCarbon DioxideCatalysisElectron TransportEnzyme ActivatorsProtein Structure, SecondaryAzurinCarbon DioxideEnzyme Activators

Identifiers

PMID27406946
PMCPMC4977188
OpenAlexW2468119604

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.