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A bacterial hydrogen-dependent CO2 reductase forms filamentous structures.

Kai Schuchmann1, Janet Vonck2, Volker Müller1

  • 1Department of Molecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University, Frankfurt am Main, Germany.

The FEBS Journal
|February 3, 2016
PubMed
Summary
This summary is machine-generated.

A novel enzyme complex in bacteria reversibly reduces carbon dioxide using hydrogen. This oxygen-sensitive enzyme polymerizes into active filaments, a rare but increasingly observed phenomenon in metabolic enzymes.

Keywords:
acetogencarbon dioxide reductioncarbon fixationformate dehydrogenasehydrogenase

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Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • The Wood-Ljungdahl pathway is crucial for carbon fixation and energy conservation in acetogenic bacteria.
  • Interconversion of carbon dioxide (CO2) and formic acid is a key bacterial metabolic process.
  • A novel enzyme complex utilizing molecular hydrogen for CO2 reduction has been identified.

Purpose of the Study:

  • To further characterize the quaternary structure of the novel enzyme complex.
  • To investigate the enzyme's unexpected polymerization into filamentous structures.
  • To understand the relationship between polymerization, enzymatic activity, and environmental conditions.

Main Methods:

  • Biochemical characterization of the enzyme complex.
  • Analysis of quaternary structure.
  • Observation of enzyme polymerization under varying conditions, including the presence of divalent cations.
  • Assessment of enzymatic activity in both monomeric and filamentous forms.

Main Results:

  • The enzyme complex exhibits polymerization into ordered filaments exceeding 0.1 μm in length.
  • Filament formation is dependent on the presence of divalent cations.
  • Polymerization is a reversible process.
  • The filamentous form of the enzyme demonstrates heightened enzymatic activity.
  • The enzyme is oxygen-sensitive, with polymerization linked to its activity.

Conclusions:

  • Metabolic enzymes can polymerize into filamentous structures, a phenomenon observed in rare cases but potentially more general.
  • The polymerization of this CO2-reducing enzyme is reversible and enhances its activity.
  • Divalent cations are key regulators of this enzyme's polymerization process.
  • Understanding enzyme polymerization offers new insights into enzyme functioning and metabolic regulation.