Evidence map›Paper›PMID 28062838›Full record

ReviewThe Biochemical journal2017

Enzymes as modular catalysts for redox half-reactions in H2-powered chemical synthesis: from biology to technology.

Holly A Reeve, Philip A Ash, HyunSeo Park, Ailun Huang, Michalis Posidias, Chloe Tomlinson, Oliver Lenz, Kylie A Vincent

Open access · hybridAbstract readReview
In one paragraph

Review in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 59 citations in OpenAlex.

  1. Electroenzymatic COAngewandte Chemie (International ed. in English) · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. HydG, the "dangler" iron, and catalytic production of free CO and CNDalton transactions (Cambridge, England : 2003) · 2021
    Article
  9. Article
  10. Article
  11. Carbon as a Simple Support for Redox Biocatalysis in Continuous Flow.Organic process research & development · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

8 authors at 1 institution in 1 country.

Holly A ReeveDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K.
Philip A AshDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K.
HyunSeo ParkDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K.
Ailun HuangDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K.
Michalis PosidiasDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K.
Chloe TomlinsonDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K.
Oliver LenzDepartment of Chemistry, Technische Universität Berlin, Berlin 10623, Germany.
Kylie A VincentDepartment of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, Oxford, OX1 3QR, U.K. kylie.vincent@chem.ox.ac.uk.
Technische Universität Berlin · DE

Funding

Biotechnology and Biological Sciences Research Council BB/L009722/1Biotechnology and Biological Sciences Research Council BB/L013711/1Biotechnology and Biological Sciences Research Council BB/M017095/1
6 · The paper itself

Abstract

The present study considers the ways in which redox enzyme modules are coupled in living cells for linking reductive and oxidative half-reactions, and then reviews examples in which this concept can be exploited technologically in applications of coupled enzyme pairs. We discuss many examples in which enzymes are interfaced with electronically conductive particles to build up heterogeneous catalytic systems in an approach which could be termed synthetic biochemistry We focus on reactions involving the H

Indexed as

Bacterial ProteinsBiocatalysisBiofuelsBiotechnologyCoenzymesElectrochemistryHydrogenHydrogenaseLightNADOxidation-ReductionPhotochemical ProcessesProtein EngineeringBacterial ProteinsBiofuelsCoenzymesHydrogenHydrogenaseNADnickel-iron hydrogenasebiotechnologyheterogeneous catalysishydrogenhydrogenaseNADHredox enzymes

Identifiers

PMID28062838
PMCPMC5298933
OpenAlexW2568952455

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.