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Reversible enzyme-catalysed NAD+/NADH electrochemistry.

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Formate dehydrogenase subcomplex FdsBG from Cupriavidus necator reversibly interconverts NAD+/NADH. Electrochemical analysis determined kinetic properties and rate constants for this NADH dehydrogenase enzyme.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioenergetics

Background:

  • Formate dehydrogenase (FdsDABG) from Cupriavidus necator is a molybdenum-containing enzyme.
  • It catalyzes formate oxidation to CO2 and CO2 reduction to formate using NAD+ or NADH.
  • FdsDABG belongs to the NADH dehydrogenase superfamily.

Purpose of the Study:

  • To electrochemically characterize the FdsBG subcomplex, which lacks the Mo-cofactor but contains FMN and iron-sulfur clusters.
  • To determine the redox potentials of the cofactors within FdsBG.
  • To elucidate the kinetic and mechanistic properties of NAD+/NADH interconversion.

Main Methods:

  • UV-vis spectroelectrochemistry to determine cofactor redox potentials (pH 6-8).
  • Cyclic voltammetry to investigate oxidation and reduction half-reactions.
  • Mediated enzyme electrochemistry with redox mediators (methylene blue, methyl viologen) to determine kinetic parameters.

Main Results:

  • Redox potentials of FMN, [2Fe-2S], and [4Fe-4S] clusters were determined.
  • Michaelis constant for NADH oxidation (KM,NADH) was 1.7 × 10^2 μM.
  • Michaelis constant for NAD+ reduction (KM,NAD) was 1.2 mM.
  • Electrochemical simulations reproduced experimental data, yielding self-consistent rate constants.

Conclusions:

  • This study provides the first electrochemical kinetic analysis of a reversible NADH dehydrogenase enzyme.
  • The findings offer new insights into the catalytic mechanism of the FdsDABG formate dehydrogenase holoenzyme.
  • The kinetic data are crucial for understanding the enzyme's role in cellular redox balance.