Evidence map›Paper›PMID 28637918›Full record

ReviewJournal of the Royal Society, Interface2017

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality.

Ross D Milton, Shelley D Minteer

Abstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Surface Immobilization of Metalloenzymes Usinga Pyrene-Modified Hydrogel.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Review
  7. Article
  8. Understanding the role of negative charge in the scaffold of an artificial enzyme for COJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Interface engineering of cellobiose dehydrogenase improves interdomain electron transfer.Protein science : a publication of the Protein Society · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. 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.

Ross D MiltonDepartment of Chemistry, University of Utah, 315 S 1400 E, Room 2020, Salt Lake City, UT 84112, USA.ORCID 0000-0002-2229-0243
Shelley D MinteerDepartment of Chemistry, University of Utah, 315 S 1400 E, Room 2020, Salt Lake City, UT 84112, USA minteer@chem.utah.edu.ORCID 0000-0002-5788-2249

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic bioelectrocatalysis is being increasingly exploited to better understand oxidoreductase enzymes, to develop minimalistic yet specific biosensor platforms, and to develop alternative energy conversion devices and bioelectrosynthetic devices for the production of energy and/or important chemical commodities. In some cases, these enzymes are able to electronically communicate with an appropriately designed electrode surface without the requirement of an electron mediator to shuttle electrons between the enzyme and electrode. This phenomenon has been termed direct electron transfer or direct bioelectrocatalysis. While many thorough studies have extensively investigated this fascinating feat, it is sometimes difficult to differentiate desirable enzymatic bioelectrocatalysis from electrocatalysis deriving from inactivated enzyme that may have also released its catalytic cofactor. This article will review direct bioelectrocatalysis of several oxidoreductases, with an emphasis on experiments that provide support for direct bioelectrocatalysis versus denatured enzyme or dissociated cofactor. Finally, this review will conclude with a series of proposed control experiments that could be adopted to discern successful direct electronic communication of an enzyme from its denatured counterpart.

Indexed as

Electrochemical TechniquesElectrophysiological PhenomenaBiosensing TechniquesCatalysisOxidoreductasesProtein ConformationOxidoreductasesbioelectrochemistrybiofuel cellbiosensordirect electron transfer

Identifiers

PMID28637918
PMCPMC5493807

What OpenQuestion holds

Textmetadata
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.