Spectroscopic and Electrochemical Characterization of the [NiFeSe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F: Reversible Redox Behavior and Interactions between Electron Transfer Centers

Authors

  • Dr. Jana Riethausen,

    1. Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
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  • Dr. Olaf Rüdiger,

    1. Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
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  • Prof. Dr. Wolfgang Gärtner,

    1. Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
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  • Prof. Dr. Wolfgang Lubitz,

    Corresponding author
    1. Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
    • Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
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  • Dr. Hannah S. Shafaat

    Corresponding author
    1. Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
    • Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, Muelheim an der Ruhr 45470 (Germany)
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Abstract

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Characterizing a new hydrogenase: The newly isolated [NiFeSe] hydrogenase from Desulfovibrio vulgaris Miyazaki F displays catalytic properties distinct from other hydrogenase proteins. Here we apply site-specific spectroscopic and electrochemical techniques to characterize these unique features at the molecular level.

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