Evidence map›Paper›PMID 31008015›Full record

ReviewChemElectroChem2019

Direct Electron Transfer of Enzymes Facilitated by Cytochromes.

Su Ma, Roland Ludwig

Open access · hybridAbstract readReview
In one paragraph

Review in ChemElectroChem, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Reducing Flavin and Ubiquinone Headgroups with Silicon Nanowire Photocathodes.Artificial photosynthesis (Washington, D.C.) · 2026
    Article
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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.

Su MaBiocatalysis and Biosensing Laboratory Department of Food Science and Technology BOKU - University of Natural Resources and Life Sciences Muthgasse 18 1190 Vienna Austria.ORCID 0000-0003-2438-7222
Roland LudwigBiocatalysis and Biosensing Laboratory Department of Food Science and Technology BOKU - University of Natural Resources and Life Sciences Muthgasse 18 1190 Vienna Austria.ORCID 0000-0002-5058-5874
BOKU University · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The direct electron transfer (DET) of enzymes has been utilized to develop biosensors and enzymatic biofuel cells on micro- and nanostructured electrodes. Whereas some enzymes exhibit direct electron transfer between their active-site cofactor and an electrode, other oxidoreductases depend on acquired cytochrome domains or cytochrome subunits as built-in redox mediators. The physiological function of these cytochromes is to transfer electrons between the active-site cofactor and a redox partner protein. The exchange of the natural electron acceptor/donor by an electrode has been demonstrated for several cytochrome carrying oxidoreductases. These multi-cofactor enzymes have been applied in third generation biosensors to detect glucose, lactate, and other analytes. This review investigates and classifies oxidoreductases with a cytochrome domain, enzyme complexes with a cytochrome subunit, and covers designed cytochrome fusion enzymes. The structurally and electrochemically best characterized proponents from each enzyme class carrying a cytochrome, that is, flavoenzymes, quinoenzymes, molybdenum-cofactor enzymes, iron-sulfur cluster enzymes, and multi-haem enzymes, are featured, and their biochemical, kinetic, and electrochemical properties are compared. The cytochromes molecular and functional properties as well as their contribution to the interdomain electron transfer (IET, between active-site and cytochrome) and DET (between cytochrome and electrode) with regard to the achieved current density is discussed. Protein design strategies for cytochrome-fused enzymes are reviewed and the limiting factors as well as strategies to overcome them are outlined.

Indexed as

cytochromedirect electrochemistrydirect electron transferflavinflavocytochromehaemiron-sulfur clustermolybdenummulti-cofactor enzymepyrrolinoquinoline quinone

Identifiers

PMID31008015
PMCPMC6472588
OpenAlexW2901214526

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.