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Fast reactions occurring in times shorter than the time needed to mix reactants pose a unique challenge for investigation. In a liquid-phase continuous-flow system, reactants A and B are swiftly pushed into the mixing chamber, where mixing occurs within 1 ms. The reaction mixture then flows through an observation tube, and one measures light absorption to determine species concentrations at various points of the tube. This method is most appropriate when relatively large volumes of reactants...
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Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1
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Breaking the barrier to fast electron transfer.

Soren Demin1, Elizabeth A H Hall

  • 1Institute of Biotechnology, Department of Chemical Engineering and Biotechnology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QT, United Kingdom.

Bioelectrochemistry (Amsterdam, Netherlands)
|April 9, 2009
PubMed
Summary
This summary is machine-generated.

Researchers studied electron transfer in a non-glycosylated glucose oxidase (GOx) enzyme. Immobilizing GOx enabled faster electron transfer than free flavin adenine dinucleotide (FAD), with oxygen impacting the rate.

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Area of Science:

  • Biophysical Chemistry
  • Electrochemistry
  • Enzyme Kinetics

Background:

  • Glucose oxidase (GOx) is a crucial enzyme for biosensing applications.
  • Understanding electron transfer (ET) mechanisms in GOx is vital for optimizing biosensor performance.
  • Enzyme immobilization strategies can influence ET rates by controlling enzyme-electrode distance.

Purpose of the Study:

  • To investigate direct electrochemical electron transfer (ET) of a non-glycosylated GOx variant.
  • To determine the influence of enzyme immobilization on ET rates.
  • To explore the effect of oxygen on GOx ET kinetics and active site mechanisms.

Main Methods:

  • Immobilization of a non-glycosylated GOx variant onto an electrode using a polyhistidine tag.
  • Electrochemical measurements (cyclic voltammetry) under anaerobic and aerobic conditions.
  • Kinetic analysis of electron transfer rates using Marcus theory predictions.

Main Results:

  • Achieved direct, rapid, and reversible electrochemical ET with a rate constant of ~350 s⁻¹ (anaerobic).
  • Demonstrated ET rates two orders of magnitude faster than free flavin adenine dinucleotide (FAD).
  • Observed reduced ET rate (~160 s⁻¹) in the presence of oxygen, potentially due to histidine interactions.

Conclusions:

  • Non-glycosylated GOx immobilization facilitates significantly enhanced direct electron transfer.
  • The conformation of FAD within the GOx active site plays a critical role in ET efficiency.
  • Oxygen presence attenuates direct ET rates, suggesting a role in modulating protein electron transfer pathways.