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Coenzyme Coupling Boosts Charge Transport through Single Bioactive Enzyme Junctions.

Xiaoyan Zhuang1, Aihui Zhang1, Siyao Qiu2

  • 1State Key Laboratory of Physical Chemistry of Solid Surfaces, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, China; The Key Laboratory for Chemical Biology of Fujian Province, Key Lab for Synthetic Biotechnology of Xiamen City, Xiamen University, Xiamen 361005, China.

Iscience
|April 8, 2020
PubMed
Summary
This summary is machine-generated.

Formate dehydrogenase (FDH) enzyme activity and charge transport were investigated. Coupling FDH with nicotinamide adenine dinucleotide (NAD+) significantly boosted charge transport and enzyme activity, revealing a link between bioactivity and electron transfer.

Keywords:
Analytical ChemistryBiotechnologyMolecular Biology

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Area of Science:

  • Biophysics
  • Enzyme catalysis
  • Molecular electronics

Background:

  • Formate dehydrogenase (FDH) catalyzes formate oxidation to CO2 via electron transfer to nicotinamide adenine dinucleotide (NAD+).
  • Understanding charge transport mechanisms in single enzymes is crucial for bioelectronic applications.
  • The charge transport characteristics of FDH remain largely unexplored.

Purpose of the Study:

  • To investigate charge transport through single-enzyme junctions of FDH.
  • To explore the role of nicotinamide adenine dinucleotide (NAD+) coupling in FDH charge transport and activity.
  • To establish a correlation between single-enzyme conductance and enzyme activity.

Main Methods:

  • Scanning tunneling microscope break junction (STM-BJ) technique was employed to form single-enzyme junctions.
  • Flicker noise analysis was used to study charge transport pathways.
  • Computational methods were used to calculate the HOMO-LUMO gap.
  • Site-specific mutagenesis was performed to analyze enzyme variants.

Main Results:

  • Coupling of NAD+ with FDH enhanced charge transport by approximately 2,100%.
  • Single-enzyme conductance strongly correlated with FDH enzyme activity.
  • Flicker noise analysis revealed switching in the coenzyme-mediated charge transport pathway.
  • Mutagenesis confirmed that FDH-NAD+ complexes exhibit enhanced bioactivity and charge transport, optimized through natural selection.

Conclusions:

  • The study provides evidence for hydrogen bond coupling influencing bioactivity.
  • A direct link between charge transport in single-enzyme junctions and enzyme activity was established.
  • Optimized coenzyme coupling significantly boosts both enzyme activity and charge transport efficiency.