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A Functional Model for the Rieske Center: Full Characterization of a Biomimetic N-Ligated [2Fe-2S] Cluster in Different Protonation States

Authors

  • Antonia Albers,

    1. Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany), Fax: (+49) 0551-39-33063
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  • Thomas Bayer,

    1. Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany), Fax: (+49) 0551-39-33063
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  • Dr. Serhiy Demeshko,

    1. Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany), Fax: (+49) 0551-39-33063
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  • Dr. Sebastian Dechert,

    1. Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany), Fax: (+49) 0551-39-33063
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  • Prof. Dr. Franc Meyer

    Corresponding author
    1. Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany), Fax: (+49) 0551-39-33063
    • Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany), Fax: (+49) 0551-39-33063

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Abstract

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Give and take both: A bis(benzimidazolate)-capped biomimetic [2Fe-2S] cluster has been characterized in different protonation states, both in the diferric and mixed-valent forms. Protonation does not lead to structural changes of the [2Fe-2S] core, but facilitates its reduction and causes pronounced valence localization in the mixed-valent state. Concerted proton and electron transfer back to the diferric cluster emulates a key step in the function of mitochondrial Rieske proteins (see scheme).

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