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Related Experiment Videos

Fe-only hydrogenases: structure, function and evolution.

Yvain Nicolet1, Christine Cavazza, J C Fontecilla-Camps

  • 1Laboratoire de Cristallographie et de Cristallogenèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF, 41, rue Jules Horowitz, 38027 Grenoble, Cedex 1, France.

Journal of Inorganic Biochemistry
|July 18, 2002
PubMed
Summary

Fe-hydrogenases, a simpler enzyme class, have an identified active site and proposed pathways for hydrogen, electron, and proton transfer. Eukaryotes possess homologous sequences, suggesting broader biological roles for these iron-only hydrogenase enzymes.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Hydrogenases catalyze reversible hydrogen reactions (H2 <==> 2H+ + 2e-).
  • Major classes include Nickel-Iron (NiFe) and Iron-only (Fe-only) hydrogenases.
  • Both classes share an unusual active site with low-spin Fe coordinated by CO and CN.

Purpose of the Study:

  • Focus on Fe-hydrogenases due to their structural simplicity compared to NiFe counterparts.
  • Identify the primary hydrogen binding site and propose catalytic pathways.
  • Compare Fe-hydrogenases with related eukaryotic proteins.

Main Methods:

  • Spectroscopic studies
  • Electrochemical studies
  • Structural studies
  • Genome sequencing analysis

Related Experiment Videos

  • Structural comparison

    • Main Results:

    • Identified the primary hydrogen binding site in Fe-hydrogenases.
    • Proposed plausible pathways for hydrogen, electron, and proton transfer.
    • Discovered homologous gene sequences in eukaryotes (yeast, plants, worms, insects, mammals).

    Conclusions:

    • Fe-hydrogenases represent a simpler model for understanding hydrogenase mechanisms.
    • Structural data provides insights into catalytic pathways.
    • Homology suggests potential roles for Fe-hydrogenases or related proteins across diverse eukaryotic organisms.