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Direct enzymatic bioelectrocatalysis: differentiating between myth and reality.

Ross D Milton1, Shelley D Minteer2

  • 1Department of Chemistry, University of Utah, 315 S 1400 E, Room 2020, Salt Lake City, UT 84112, USA.

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|June 23, 2017
PubMed
Summary

Direct bioelectrocatalysis enables enzymes to communicate directly with electrodes. This review distinguishes true enzymatic activity from denatured enzyme electrocatalysis, proposing controls for accurate assessment.

Keywords:
bioelectrochemistrybiofuel cellbiosensordirect electron transfer

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Area of Science:

  • Biochemistry
  • Electrochemistry
  • Bioengineering

Background:

  • Enzymatic bioelectrocatalysis utilizes oxidoreductase enzymes for biosensors and bioelectrosynthetic devices.
  • Direct electron transfer (DET) allows enzymes to communicate electronically with electrodes without mediators.
  • Distinguishing DET from denatured enzyme activity is crucial for reliable applications.

Purpose of the Study:

  • To review direct bioelectrocatalysis of oxidoreductases.
  • To highlight experimental evidence differentiating true DET from denatured enzyme electrocatalysis.
  • To propose control experiments for validating direct electronic communication.

Main Methods:

  • Literature review of studies on direct bioelectrocatalysis in oxidoreductases.
  • Analysis of experimental data supporting direct electron transfer.
  • Evaluation of methods to distinguish active enzyme from denatured enzyme or cofactor release.

Main Results:

  • Direct bioelectrocatalysis is a key phenomenon in enzyme-electrode interactions.
  • Several studies provide evidence for direct electron transfer in oxidoreductases.
  • Challenges remain in differentiating true DET from artifacts of denatured enzymes or released cofactors.

Conclusions:

  • Accurate differentiation between direct bioelectrocatalysis and denatured enzyme activity is essential.
  • Proposed control experiments can help validate direct electronic communication.
  • Further research is needed to refine methods for assessing enzyme-electrode interfaces.