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Correction: Tallarita et al. The Role of -OEt Substituents in Molybdenum-Assisted Pentathiepine Formation-Access to Diversely Functionalized Azines. <i>Molecules</i> 2024, <i>29</i>, 3806.

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Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
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In vitro sulfuration of Rhodobacter capsulatus formate dehydrogenase.

Benjamin R Duffus1, Benedict J Elvers2, Christian Teutloff3

  • 1Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, Potsdam, Germany.

The Journal of Biological Chemistry
|April 17, 2025
PubMed
Summary

This study demonstrates in vitro sulfido ligand incorporation to restore activity in metal-dependent formate dehydrogenases (FDHs). This method reactivates the enzyme, crucial for CO2 reduction and formate production.

Keywords:
carbon dioxidedithioniteformatehydrogen sulfideiron-sulfur proteinmolybdenumsulfursulfur transfertungsten

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Metal-dependent formate dehydrogenases (FDHs) are key enzymes for CO2 reduction to formate.
  • FDHs contain an active site sulfido ligand essential for activity but sensitive to oxygen.
  • Current methods use inhibitors to protect the active site from oxidative damage.

Purpose of the Study:

  • To investigate in vitro sulfido ligand incorporation into the bis-MGD cofactor of Rhodobacter capsulatus FDH.
  • To explore a method for reactivating FDHs and understanding the role of the sulfido ligand.

Main Methods:

  • In vitro sulfido ligand incorporation using sulfide, bisulfite, or sodium dithionite under anaerobic, weakly acidic conditions.
  • Enzymatic activity assays.
  • Electron Paramagnetic Resonance (EPR) spectroscopy to confirm sulfido ligand and Mo coordination.

Main Results:

  • Successful in vitro sulfido ligand incorporation completely reactivated FDH activity.
  • Reactivated enzyme showed activity comparable to heterologously expressed FDH.
  • EPR spectroscopy confirmed MoS6 coordination and the role of the 33S sulfido ligand in the MoV-SH state.

Conclusions:

  • In vitro sulfido ligand incorporation is a viable method to reactivate FDHs.
  • The sulfido ligand is critical for the electronic properties of the MoV-SH state in the bis-MGD cofactor.
  • This finding has implications for understanding and engineering other molybdoenzymes.