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Electrochemical Detection of Deuterium Kinetic Isotope Effect on Extracellular Electron Transport in Shewanella oneidensis MR-1

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Downsizing effect on direct electron transfer-type bioelectrocatalysis by d-fructose dehydrogenase with structural

Yohei Suzuki¹, Yuki Kitazumi¹, Osamu Shirai¹

¹Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto, Japan.

Bioscience, Biotechnology, and Biochemistry

|March 27, 2025

Summary

Downsizing Gluconobacter japonicus d-fructose dehydrogenase (FDH) by removing heme c moieties significantly boosts direct electron transfer (DET) bioelectrocatalysis. Variants showed 7-fold and 4-fold faster electron transfer rates, respectively.

Keywords:

d-fructose dehydrogenase direct electron transfer downsizing non-catalytic redox signal structural prediction

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Published on: December 4, 2017

Area of Science:

Biochemistry
Bioelectrochemistry
Enzyme Engineering

Background:

Membrane-bound heterotrimeric d-fructose dehydrogenase (FDH) from Gluconobacter japonicus displays direct electron transfer (DET)-type bioelectrocatalytic activity.
FDH possesses three heme c moieties; variants lacking heme 1c (Δ1c FDH) or hemes 1c and 2c (Δ1c2c FDH) were previously constructed.

Purpose of the Study:

To quantitatively analyze the impact of downsizing FDH variants (Δ1c FDH and Δ1c2c FDH) on DET-type bioelectrocatalysis.
To evaluate kinetic parameters and electron transfer rates of FDH variants.

Main Methods:

Construction of downsized FDH variants (Δ1c FDH, Δ1c2c FDH).
Electrochemical analysis to obtain non-catalytic redox signals and DET-type catalytic waves.
Quantitative analysis of kinetic parameters and electron transfer rate constants.

Main Results:

Non-catalytic redox signals of adsorbed enzymes were successfully obtained.
Electron transfer rate constants were enhanced by 7-fold for Δ1c FDH and 4-fold for Δ1c2c FDH.
Downsizing effect on bioelectrocatalysis was quantitatively analyzed.

Conclusions:

FDH downsizing significantly enhances DET-type bioelectrocatalytic activity.
Structural predictions correlate with observed acceleration factors in variants.
This study provides insights into enzyme engineering for improved bioelectrocatalysis.