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Assessing Lanthanide-Dependent Methanol Dehydrogenase Activity: The Assay Matters.

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|January 25, 2024
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Summary

This study cultivated lanthanide-dependent methanotrophs with various lanthanides to assess methanol dehydrogenase (MDH) activity. Protein-coupled assays revealed early lanthanides enhance MDH interaction with its physiological partner, improving functional efficiency.

Keywords:
lanthanide-dependent bacterialanthanidesmetalloenzymesmethanol dehydrogenasemethylotrophy

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Methanol dehydrogenases (MDH) are crucial enzymes, often assessed using artificial dye-coupled assays.
  • Lanthanide (Ln)-dependent XoxF-MDHs can incorporate different Lns, with dye assays suggesting early Lns yield higher activity.
  • Current methods require specific pH and activators, and Ln-MDH variants are typically generated in vitro, not via direct cultivation.

Purpose of the Study:

  • To investigate the cultivation of Ln-dependent methanotrophs with various Lns.
  • To assess the activity of isolated Ln-MDHs using both dye-coupled and protein-coupled assays.
  • To compare enzyme activity trends between the two assay types and understand Ln effects on enzyme-substrate interactions.

Main Methods:

  • Cultivation of Methylacidiphilum fumariolicum SolV with nine different Lns.
  • Isolation of the respective Ln-dependent XoxF-MDH variants.
  • Enzyme activity assessment using traditional dye-coupled assays and a protein-coupled assay with cytochrome cGJ (cyt cGJ).

Main Results:

  • Two distinct activity trends were observed depending on the assay method used.
  • The protein-coupled assay showed higher specific enzyme activity for La-, Ce-, and Pr-MDH compared to the dye-coupled assay.
  • Early Lns (La, Ce, Pr) appear to positively influence the interaction between XoxF-MDH and its physiological electron acceptor, cyt cGJ.

Conclusions:

  • Direct cultivation and isolation of Ln-MDHs provide insights into their activity.
  • The choice of assay significantly impacts the observed trends in Ln-MDH activity.
  • Early lanthanides enhance the functional efficiency of XoxF-MDH by promoting interaction with its native electron acceptor.