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Resonance Raman studies of iron-only hydrogenases

W Fu1, P M Drozdzewski, T V Morgan

  • 1Department of Chemistry, University of Georgia, Athens 30602.

Biochemistry
|May 11, 1993
PubMed
Summary

Resonance Raman spectroscopy revealed diverse iron-sulfur clusters in Fe-only hydrogenases. Findings suggest the hydrogen activating center in Clostridium pasteurianum hydrogenase I is a novel iron center, not a typical iron-sulfur cluster.

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Area of Science:

  • Biochemistry
  • Spectroscopy
  • Bioinorganic Chemistry

Background:

  • Iron-only hydrogenases are crucial enzymes catalyzing hydrogen oxidation and production.
  • Understanding the structure and function of their iron-sulfur clusters is key to elucidating their catalytic mechanisms.
  • Previous studies suggested specific iron-sulfur cluster compositions in various hydrogenases.

Purpose of the Study:

  • To investigate the iron-sulfur clusters in oxidized and reduced Fe-only hydrogenases from Desulfovibrio vulgaris, Thermotoga maritima, and Clostridium pasteurianum.
  • To clarify the composition of iron-sulfur clusters, particularly in Clostridium pasteurianum hydrogenase I.
  • To identify the nature of the hydrogen activating center in these enzymes.

Main Methods:

  • Resonance Raman spectroscopy was employed to analyze the iron-sulfur clusters.

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  • Spectroscopic data was collected for both oxidized and reduced forms of the hydrogenases.
  • Comparative analysis was performed across hydrogenases from different microbial sources.

    • Main Results:

    • Ferredoxin-like [4Fe-4S]2+,+ and [2Fe-2S]2+,+ clusters were identified in Thermotoga maritima and Clostridium pasteurianum hydrogenase I.
    • [4Fe-4S]2+,+ clusters were the only type found in Desulfovibrio vulgaris hydrogenase.
    • Resonance Raman bands previously attributed to the hydrogen activating center in C. pasteurianum hydrogenase I were reassigned to an indigenous [2Fe-2S]2+ cluster.

    Conclusions:

    • The iron-sulfur cluster composition of Clostridium pasteurianum hydrogenase I requires reevaluation.
    • The hydrogen activating center in these Fe-only hydrogenases does not exhibit resonance Raman bands characteristic of known iron-sulfur clusters.
    • This suggests the hydrogen activating center is a novel iron center, distinct from conventional iron-sulfur clusters.